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High-affinity PQQ import is widespread in Gram-negative bacteria
Open accessPublished version of a preprint
Abstract
Pyrroloquinoline quinone (PQQ) is a soluble redox cofactor used by diverse bacteria. Many Gram-negative bacteria that encode PQQ-dependent enzymes do not produce it and instead obtain it from the environment. To achieve this, Escherichia coli uses the TonB-dependent transporter PqqU as a high-affinity PQQ importer. Here, we show that PqqU binds PQQ with high affinity and determine the high-resolution structure of the PqqU-PQQ complex, revealing that PqqU undergoes conformational changes in PQQ binding to capture the cofactor in an internal cavity. We show that these conformational changes preclude the binding of a bacteriophage, which targets PqqU as a cell surface receptor. Guided by the PqqU-PQQ structure, we identify amino acids essential for PQQ import and leverage this information to map the presence of PqqU across Gram-negative bacteria. This reveals that PqqU is encoded by Gram-negative bacteria from at least 22 phyla occupying diverse habitats, indicating that PQQ is an important cofactor for bacteria that adopt diverse lifestyles and metabolic strategies.
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UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,882
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Kearse, M., Moir, R., Wilson, A., Stones-Havas, S., Cheung, M., Sturrock, S., Buxton, S., Cooper, A., Markowitz, S., Duran, C., et al. (2012) · Bioinform. · doi:10.1093/bioinformatics/bts199 · Cited by 19,197
trimAl: a tool for automated alignment trimming in large-scale phylogenetic analyses
Capella-Gutiérrez, S., Silla-Martinez, J., & Gabaldón, T. (2009) · Bioinform. · doi:10.1093/bioinformatics/btp348 · Cited by 12,052
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 11,626
Interactive Tree Of Life (iTOL) v5: an online tool for phylogenetic tree display and annotation
Letunic, I., & Bork, P. (2021) · Nucleic Acids Res. · doi:10.1093/nar/gkab301 · Cited by 9,915
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S. Q., Palovcak, E. J., Armache, J., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,496
Pfam: The protein families database in 2021
Mistry, J., Chuguransky, S., Williams, L., Qureshi, M., Salazar, G. A., Sonnhammer, E. L. L., Tosatto, S. C. E., Paladin, L., Raj, S., Richardson, L. J., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa913 · Cited by 7,452
CTFFIND4: Fast and accurate defocus estimation from electron micrographs
Rohou, A. L., & Grigorieff, N. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.08.008 · Cited by 4,759
Protein complex prediction with AlphaFold-Multimer
Evans, R., O’Neill, M., Pritzel, A., Antropova, N., Senior, A., Green, T., Žídek, A., Bates, R., Blackwell, S., Yim, J., et al. (2021) · doi:10.1101/2021.10.04.463034 · Cited by 3,808
SignalP 6.0 predicts all five types of signal peptides using protein language models
Teufel, F., Armenteros, J. J. A., Johansen, A. R., Gíslason, M. H., Pihl, S. I., Tsirigos, K. D., Winther, O., Brunak, S., von HEIJNE, G., & Nielsen, H. (2022) · Nature Biotechnology · doi:10.1038/s41587-021-01156-3 · Cited by 3,088
Olm, M. R., Brown, C. T., Brooks, B., & Banfield, J. F. (2017) · The ISME Journal · doi:10.1038/ismej.2017.126 · Cited by 3,031
Fast and accurate protein structure search with Foldseek
van Kempen, M., Kim, S. S., Tumescheit, C., Mirdita, M., Lee, J., Gilchrist, C. L. M., Söding, J., & Steinegger, M. (2022) · doi:10.1101/2022.02.07.479398 · Cited by 2,598
Fast and accurate protein structure search with Foldseek
van Kempen, M., Kim, S. S., Tumescheit, C., Mirdita, M., Lee, J., Gilchrist, C. L. M., Söding, J., & Steinegger, M. (2024) · Nature Biotechnology · doi:10.1038/s41587-023-01773-0 · Cited by 2,596
SignalP 6.0 predicts all five types of signal peptides using protein language models
Teufel, F., Armenteros, J. J. A., Johansen, A. R., Gíslason, M. H., Pihl, S. I., Tsirigos, K. D., Winther, O., Brunak, S., von HEIJNE, G., & Nielsen, H. (2022) · Repository for Publications and Research Data (ETH Zurich) · doi:10.3929/ethz-b-000524414 · Cited by 1,905
clinker & clustermap.js: automatic generation of gene cluster comparison figures
Gilchrist, C. L. M., & Chooi, Y. (2021) · Bioinformatics · doi:10.1093/bioinformatics/btab007 · Cited by 1,615
Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction
Punjani, A., Zhang, H., & Fleet, D. J. (2020) · Nature Methods · doi:10.1038/s41592-020-00990-8 · Cited by 1,559
Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs
Bepler, T., Morin, A., Rapp, M., Brasch, J., Shapiro, L., Noble, A., & Berger, B. (2018) · Nature Methods · doi:10.1038/s41592-019-0575-8 · Cited by 1,455
New tools for automated cryo-EM single-particle analysis in RELION-4.0
Kimanius, D., Dong, L., Sharov, G., Nakane, T., & Scheres, S. H. W. (2021) · Biochemical Journal · doi:10.1042/bcj20210708 · Cited by 1,095
A Bayesian approach to beam-induced motion correction in cryo-EM single-particle analysis
Zivanov, J., Nakane, T., & Scheres, S. H. W. (2018) · IUCrJ · doi:10.1107/s205225251801463x · Cited by 947
Zivanov, J., Nakane, T., & Scheres, S. H. W. (2020) · IUCrJ · doi:10.1107/s2052252520000081 · Cited by 804
Chai-1: Decoding the molecular interactions of life
Discovery, C., Boitreaud, J., Dent, J., McPartlon, M., Meier, J., Reis, V., Rogozhnikov, A., & Wu, K. (2024) · doi:10.1101/2024.10.10.615955 · Cited by 517
PQQ-dependent methanol dehydrogenases: rare-earth elements make a difference
Keltjens, J. T., Pol, A., Reimann, J., & den Camp, H. J. M. O. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5766-8 · Cited by 415
Systematic exploration of Escherichia coli phage–host interactions with the BASEL phage collection
Maffei, E., Shaidullina, A., Burkolter, M., Heyer, Y., Estermann, F., Druelle, V., Sauer, P., Willi, L., Michaelis, S., Hilbi, H., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001424 · Cited by 298
CheckMyMetal: a macromolecular metal-binding validation tool
Zheng, H.-P., Cooper, D., Porebski, P., Shabalin, I., Handing, K., & Minor, W. (2017) · Acta Crystallographica Section D: Structural Biology · doi:10.1107/s2059798317001061 · Cited by 290
Gilchrist, C. L. M., Booth, T., van Wersch, B., van Grieken, L., Medema, M. H., & Chooi, Y. (2021) · Bioinformatics Advances · doi:10.1093/bioadv/vbab016 · Cited by 283
Asarnow, D., Palovcak, E., & Cheng, Y. (2019) · Figshare · doi:10.5281/zenodo.3576629 · Cited by 241
Diamond, S., Andeer, P. F., Li, Z., Crits‐Christoph, A., Burstein, D. E., Anantharaman, K., Lane, K. R., Thomas, B. C., Pan, C., Northen, T. R., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0449-y · Cited by 221
FAMSA: Fast and accurate multiple sequence alignment of huge protein families
Deorowicz, S., Debudaj-Grabysz, A., & Gudyś, A. (2016) · Scientific Reports · doi:10.1038/srep33964 · Cited by 217
Specimen Preparation for High-Resolution Cryo-EM
Passmore, L. A., & Russo, C. J. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.04.011 · Cited by 213
Wehrmann, M., Billard, P., Martin-Mériadec, A., Zegeye, A., & Klebensberger, J. (2017) · mBio · doi:10.1128/mbio.00570-17 · Cited by 207
Yue, W. W., Grizot, S., & Buchanan, S. K. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00855-6 · Cited by 200
Katz, E. Y., Schlereth, D. D., & Schmidt, H. (1994) · Journal of Electroanalytical Chemistry · doi:10.1016/0022-0728(93)03010-m · Cited by 179
Structural insight into the role of the Ton complex in energy transduction
Celia, H., Noinaj, N., Zakharov, S. D., Bordignon, E., Botos, I., Santamaría, M., Barnard, T. J., Cramer, W. A., Lloubès, R., & Buchanan, S. K. (2016) · Nature · doi:10.1038/nature19757 · Cited by 170
An, R., & Moe, L. A. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.00813-16 · Cited by 162
Quinoproteins: structure, function, and biotechnological applications
K. Matsushita, H. T. (2002) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-001-0851-1 · Cited by 154
Pyrroloquinoline Quinone (PQQ) and Quinoprotein Enzymes
Anthony, C. (2001) · Antioxidants and Redox Signaling · doi:10.1089/15230860152664966 · Cited by 150
Translating phage therapy into the clinic: Recent accomplishments but continuing challenges
Fabijan, A. P., Iredell, J. R., Danis-Wlodarczyk, K. M., Kebriaei, R., & Abedon, S. T. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002119 · Cited by 126
Goosen, N., Horsman, H. P. A., Huinen, R. G. M., & van de Putte, P. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.1.447-455.1989 · Cited by 118
Moynié, L., Milenkovic, S., Mislin, G. L. A., Gasser, V., Malloci, G., Baco, E., McCaughan, R. P., Page, M. G. P., Schalk, I. J., Ceccarelli, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11508-y · Cited by 116
Duine, J. A. (1999) · Journal of Bioscience and Bioengineering · doi:10.1016/s1389-1723(00)80002-x · Cited by 113
Butterfield, C. N., Li, Z., Andeer, P. F., Spaulding, S. E., Thomas, B. C., Singh, A., Hettich, R. L., Suttle, K. B., Probst, A. J., Tringe, S. G., et al. (2016) · PeerJ · doi:10.7717/peerj.2687 · Cited by 107
Escherichia coli is unable to produce pyrroloquinoline quinone (PQQ)
Matsushita, K., Arents, J. C., Bader, R., Yamada, M. C., Adachi, O., & Postma, P. W. (1997) · Microbiology · doi:10.1099/00221287-143-10-3149 · Cited by 99
TonB-Dependent Transport Across the Bacterial Outer Membrane
Silale, A., & van den Berg, B. (2023) · Annual Review of Microbiology · doi:10.1146/annurev-micro-032421-111116 · Cited by 97
Gating of TonB-dependent transporters by substrate-specific forced remodelling
Hickman, S. J., Cooper, R. E. M., Bellucci, L., Paci, E., & Brockwell, D. J. (2017) · Nature Communications · doi:10.1038/ncomms14804 · Cited by 72
Methanol Dehydrogenase, a PQQ-Containing Quinoprotein Dehydrogenase
Anthony, C. (2000) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/0-306-46828-x_3 · Cited by 72
Josts, I., Veith, K., & Tidow, H. (2019) · eLife · doi:10.7554/elife.48528 · Cited by 69
Biogenesis of the peptide-derived redox cofactor pyrroloquinoline quinone
Zhu, W., & Klinman, J. P. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2020.05.001 · Cited by 64
McIntire, W. S. (1998) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.18.1.145 · Cited by 64
Unexpected metabolic versatility among type II methanotrophs in the Alphaproteobacteria
Hakobyan, A., & Liesack, W. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0200 · Cited by 61
Reaction of Reduced PQQ (PQQH2) and Molecular Oxygen
Itoh, S., Ohshiro, Y., & Agawa, T. (1986) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.59.1911 · Cited by 60
Engineered PQQ-Glucose Dehydrogenase as a Universal Biosensor Platform
Guo, Z., Murphy, L. J., Stein, V., Johnston, W. A., Alcala-Perez, S., & Alexandrov, K. A. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b06342 · Cited by 58
Structural basis for host recognition and superinfection exclusion by bacteriophage T5
van den Berg, B., Silale, A., Baslé, A., Brandner, A. F., Mader, S. L., & Khalid, S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2211672119 · Cited by 53
Chen, Z., Matsushita, K., Yamashita, T., Fujii, T., Toyama, H., Adachi, O., Bellamy, H. D., & Mathews, F. S. (2002) · Structure · doi:10.2210/pdb1kv9/pdb · Cited by 51
Characterization of Quinohemoprotein Amine Dehydrogenase from Pseudomonas putida.
Adachi, O., KUBOTA, T., Hacisalihoglu, A., Toyama, H., Shinagawa, E., Duine, J. A., & Matsushita, K. (1998) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.62.469 · Cited by 47
Bhamidimarri, S. P., Young, T. R., Shanmugam, M., Söderholm, S., Baslé, A., Bumann, D., & van den Berg, B. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001446 · Cited by 44
Grinter, R., & Lithgow, T. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011018 · Cited by 43
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Matsutani, M., & Yakushi, T. (2018) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-018-9360-3 · Cited by 43
The PQQ biosynthetic operons and their transcriptional regulation in Pseudomonas aeruginosa
Gliese, N., Khodaverdi, V., & Görisch, H. (2009) · Archives of Microbiology · doi:10.1007/s00203-009-0523-6 · Cited by 39
Pyrroloquinoline Quinone Chemistry, Biology, and Biosynthesis
Cordell, G. A., & Daley, S.-K. (2022) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.1c00340 · Cited by 31
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Grinter, R., & Lithgow, T. J. (2019) · IUCrJ · doi:10.1107/s2052252519002926 · Cited by 29
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Grinter, R., Leung, P. M., Wijeyewickrema, L. C., Littler, D. R., Beckham, S. A., Pike, R. N., Walker, D., Greening, C., & Lithgow, T. J. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008435 · Cited by 27
Self-citationXiong, K., Chen, Z., Xiang, G., Wang, J., Rao, X., Hu, F., & Cong, Y. (2011) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2011.02481.x · Cited by 24
Wan, H., Xia, Y., Li, J., Kang, Z., & Zhou, J. (2016) · Frontiers of Chemical Science and Engineering · doi:10.1007/s11705-016-1580-4 · Cited by 24
Shimao, M., Onishi, S., Kato, N., & Sakazawa, C. (1989) · Applied and Environmental Microbiology · doi:10.1128/aem.55.2.275-278.1989 · Cited by 21
Grinter, R., & Lithgow, T. J. (2020) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798320004398 · Cited by 19
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Phillips, Z. N., Jennison, A. V., Whitby, P. W., Stull, T. L., Staples, M., & Atack, J. M. (2022) · FEMS Microbiology Letters · doi:10.1093/femsle/fnac064 · Cited by 9
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Xiong, K., Deng, L., Li, Z., Gong, H., Chen, J., Huang, M., Rao, X., & Cong, Y. (2024) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-024-03937-9 · Cited by 6
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Metadata
- Authors
- Munder, F., Voutsinos, M., Hantke, K., Venugopal, H., & Grinter, R.
- Affiliations
- Monash University (AU)
- The University of Queensland (AU)
- University of Tübingen (DE)
- Ramaciotti Centre for Cryo-Electron Microscopy, Monash University, Clayton, Australia.
- The University of Melbourne (AU)
- Corresponding author
- Grinter, Rhys
- Venue
- Science Advances
- Published
- 2025-05-30
- Volume
- 11
- Issue
- 22
- Pages
- eadr2753-eadr2753
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC12124388
- OpenAlex
- W4410886489
- Cited by
- 12
- References
- 73
- Citations by year
- 2026: 7 · 2025: 5
- FWCI
- 3.61
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Science Advances (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- pyrroloquinoline quinone, TonB-dependent transporters, Gram-negative bacteria, cofactor binding, protein conformational change, bacteriophage receptors, Escherichia coli, redox cofactors
- MeSH terms
- Bacterial Proteins, Escherichia coli, Gram-Negative Bacteria, Models, Molecular, Protein Binding, Protein Conformation, Escherichia coli Proteins, PQQ Cofactor
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