The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Structural Basis for Substrate Targeting and Catalysis by Fungal Polysaccharide Monooxygenases
Open accessAbstract
SUMMARY The use of cellulases remains a major cost in the production of renewable fuels and chemicals from lignocellulosic biomass. Fungi secrete copper-dependent polysaccharide monooxygenases (PMOs) that oxidatively cleave crystalline cellulose and improve the effectiveness of cellulases. However, the means by which PMOs recognize and cleave their substrates in the plant cell wall remain unclear. Here we present structures of Neurospora crassa PMO-2 and PMO-3 at 1.10 Å and 1.37 Å resolution, respectively. In the structures, dioxygen species are found in the active sites, consistent with the proposed cleavage mechanism. Structural and sequence comparisons between PMOs also reveal that the enzyme substrate-binding surfaces contain highly varied aromatic amino acid and glycosylation positions. The structures reported here provide evidence for a wide range of PMO substrate recognition patterns in the plant cell wall, including binding modes that traverse multiple glucan chains.
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Cites
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
ZDOCK: An initial‐stage protein‐docking algorithm
Chen, R., Li, L., & Weng, Z. (2003) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10389 · Cited by 1,393 · cited 2×
“Modeling of Electron Transport Pathways in PMOs Docking of the CDH heme domain from the white rot fungus Phanerochaete chrysosporium (PDB entry 1D7B) (Hallberg et al., 2000) onto N. crassa PMO-3 was performed with ZDOCK (Chen et al., 2003).”
Cited by
Copper Active Sites in Biology
Solomon, E. I., Heppner, D. E., Johnston, E. M., Ginsbach, J. W., Cirera, J., Qayyum, M., Kieber-Emmons, M. T., Kjaergaard, C. H., Hadt, R. G., & Tian, L. (2014) · Chemical Reviews · doi:10.1021/cr400327t · Cited by 1,751
Payne, C. M., Knott, B. C., Mayes, H. B., Hansson, H., Himmel, M. E., Sandgren, M., Ståhlberg, J., & Beckham, G. T. (2015) · Chemical Reviews · doi:10.1021/cr500351c · Cited by 855
Oxidative cleavage of polysaccharides by monocopper enzymes depends on H2O2
Bissaro, B., Røhr, Å. K., Müller, G., Chylenski, P., Skaugen, M., Forsberg, Z., Horn, S. J., Vaaje-Kolstad, G., & Eijsink, V. G. H. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2470 · Cited by 594
Agger, J. W., Isaksen, T., Várnai, A., Vidal-Melgosa, S., Willats, W. G. T., Ludwig, R., Horn, S. J., Eijsink, V. G. H., & Westereng, B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1323629111 · Cited by 425
Lytic Polysaccharide Monooxygenases in Biomass Conversion
Hemsworth, G. R., Johnston, E. M., Davies, G. J., & Walton, P. H. (2015) · Trends in Biotechnology · doi:10.1016/j.tibtech.2015.09.006 · Cited by 314
Metadata
- Authors
- Li, X., Beeson, W. T., Phillips, C. M., Marletta, M. A., & Cate, J. H. D.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2012-06
- Volume
- 20
- Issue
- 6
- Pages
- 1051-1061
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W1997124914
- Cited by
- 287
- References
- 3
- FWCI
- 26.42
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Li, X., Beeson, W. T., Phillips, C. M., Marletta, M. A., & Cate, J. H. D. (2012). Structural Basis for Substrate Targeting and Catalysis by Fungal Polysaccharide Monooxygenases. Structure. https://doi.org/10.1016/j.str.2012.04.002
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
