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5OYC

GH5 endo-xyloglucanase from Cellvibrio japonicus

Summary for 5OYC
Entry DOI10.2210/pdb5oyc/pdb
DescriptorCellulase, putative, cel5D, GLYCEROL, SULFATE ION, ... (7 entities in total)
Functional Keywordsendo-xyloglucanase, hydrolase
Biological sourceCellvibrio japonicus
Total number of polymer chains2
Total formula weight91952.95
Authors
Attia, M.,Nelson, C.E.,Offen, W.A.,Jain, N.,Gardner, J.G.,Davies, G.J.,Brumer, H. (deposition date: 2017-09-08, release date: 2018-02-07, Last modification date: 2024-01-17)
Primary citationAttia, M.A.,Nelson, C.E.,Offen, W.A.,Jain, N.,Davies, G.J.,Gardner, J.G.,Brumer, H.
In vitro and in vivo characterization of threeCellvibrio japonicusglycoside hydrolase family 5 members reveals potent xyloglucan backbone-cleaving functions.
Biotechnol Biofuels, 11:45-45, 2018
Cited by
PubMed Abstract: Xyloglucan (XyG) is a ubiquitous and fundamental polysaccharide of plant cell walls. Due to its structural complexity, XyG requires a combination of backbone-cleaving and sidechain-debranching enzymes for complete deconstruction into its component monosaccharides. The soil saprophyte has emerged as a genetically tractable model system to study biomass saccharification, in part due to its innate capacity to utilize a wide range of plant polysaccharides for growth. Whereas the downstream debranching enzymes of the xyloglucan utilization system of have been functionally characterized, the requisite backbone-cleaving -xyloglucanases were unresolved.
PubMed: 29467823
DOI: 10.1186/s13068-018-1039-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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数据于2024-10-30公开中

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