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Structural basis of a phosphotransferase system xylose transporter
Open accessPreprint — published as 10.1002/1873-3468.70135 · Paper page
Abstract
The bacterial phosphotransferase system (PTS) is essential for carbohydrate uptake, and IIC transporters in the system facilitate intracellular sugar transport. Here, we report the crystal and cryo-EM structures of Leminorella grimontii GatC (LgGatC), a putative xylose transporter in the IIC family, in its outward-facing state. Structural analysis indicates that the outward-facing cavity recognizes the linear form of D-xylose. A structure-based homology model of an inward-facing state supports an elevator-like sugar transport mechanism. These findings provide insights into PTS-mediated xylose transport and its potential applications in microbial engineering.
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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
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Research works printed but not linked: 41
- 10.1016/j.biotechadv.2012.03.002 · DOI
- 10.1186/s13068-020-1662-x · DOI
- 10.1016/j.ymben.2012.07.007 · DOI
- 10.1016/j.mcat.2024.114230 · DOI
- 10.1128/aem.55.8.1943-1948.1989 · DOI
- 10.1007/s00253-006-0827-2 · DOI
- 10.1016/j.ymben.2011.05.005 · DOI
- 10.1073/pnas.1311970111 · DOI
- 10.1007/s00253-013-5401-0 · DOI
- 10.1016/S0923-2508(02)01339-6 · DOI
- 10.1007/BF02193633 · DOI
- 10.1128/MMBR.69.4.608-634.2005 · DOI
- 10.1016/j.str.2016.04.003 · DOI
- 10.1073/pnas.1800647115 · DOI
- 10.1038/nature09939 · DOI
- 10.1038/nsmb.2975 · DOI
- 10.1038/s41421-018-0037-y · DOI
- 10.1038/s41422-019-0194-z · DOI
- 10.1038/s41467-024-52100-3 · DOI
- 10.1016/j.str.2006.01.013 · DOI
- 10.1016/S0076-6879(09)64011-8 · DOI
- 10.1074/jbc.M113.485896 · DOI
- 10.1021/acs.biochem.7b00777 · DOI
- 10.1128/jb.178.23.6790-6795.1996 · DOI
- 10.1128/jb.124.1.26-38.1975 · DOI
- 10.1016/j.jsb.2016.10.002 · DOI
- 10.1093/nar/gky427 · DOI
- 10.1093/nar/gkr703 · DOI
- 10.1093/protein/14.12.993 · DOI
- 10.1038/nprot.2009.31 · DOI
- 10.1107/S2059798318017795 · DOI
- 10.1107/S2059798318004576 · DOI
- 10.1107/S0907444909047337 · DOI · Paper page
- 10.1107/S0021889807021206 · DOI · Paper page
- 10.1002/prot.26257 · DOI
- 10.1107/S0907444910007493 · DOI · Paper page
- 10.1107/S0907444909052925 · DOI · Paper page
- 10.1016/j.jsb.2005.07.007 · DOI
- 10.1038/nmeth.4169 · DOI · Paper page
- 10.1038/s41586-024-07487-w · DOI · Paper page
- 10.1002/pro.3943 · DOI
Metadata
- Authors
- Takahashi, Y. S., Kohga, H., Chek, M. F., Yamamoto, K., Takahashi, J. F., Shigematsu, H., Tanaka, Y., Ichikawa, M., Miyazaki, R., Hakoshima, T., & Tsukazaki, T.
- Affiliations
- Nara Institute of Science and Technology (JP)
- Japan Synchrotron Radiation Research Institute (JP)
- Fudan University (CN)
- Corresponding author
- Tsukazaki, Tomoya
- ORCID
- Venue
- FEBS Letters
- Publisher
- openRxiv
- Published
- 2025-04-03
- Volume
- 599
- Issue
- 16
- Pages
- 2377-2387
- ISSN
- 0014-5793 (ISSN-L)
- OpenAlex
- W4413002686
- Cited by
- 1
- References
- 1
- Citations by year
- 2026: 1
- FWCI
- 0.21
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- FEBS Letters (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (acceptedVersion)
- Funders
- Natural Science Foundation of Shanghai (24ZR1403800)
- Takeda Science Foundation
- Japan Agency for Medical Research and Development (JP24ama121001)
- Ministry of Education, Culture, Sports, Science and Technology
- Japan Society for the Promotion of Science (22K15061, JP22H02567, 22H05567)
- Precursory Research for Embryonic Science and Technology
- Chemo-Sero-Therapeutic Research Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- galactitol, transporter conformation, substrate recognition, sugar transport, homology model
- MeSH terms
- Bacterial Proteins, Models, Molecular, Phosphoenolpyruvate Sugar Phosphotransferase System, Protein Conformation, Xylose, Crystallography, X-Ray, Cryoelectron Microscopy, Planctomycetales
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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