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7TVP

Viral AMG chitosanase V-Csn, E157Q mutant, chitotriose complex

Summary for 7TVP
Entry DOI10.2210/pdb7tvp/pdb
Related7TVL 7TVM 7TVN 7TVO
DescriptorViral chitosanase V-Csn E157Q mutant chitotriose complex, 2-amino-2-deoxy-beta-D-glucopyranose-(1-4)-2-amino-2-deoxy-beta-D-glucopyranose-(1-4)-2-amino-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (4 entities in total)
Functional Keywordsglycosyl hydrolase, chitosanase, viral auxiliary metabolic gene, mutant, chitosan complex, hydrolase
Biological sourceunclassified sequences
Total number of polymer chains1
Total formula weight24756.14
Authors
Smith, C.A.,Wu, R.,Buchko, G.W.,Cort, J.R.,Hofmockel, K.S.,Jansson, J.K. (deposition date: 2022-02-05, release date: 2022-10-05, Last modification date: 2023-10-18)
Primary citationWu, R.,Smith, C.A.,Buchko, G.W.,Blaby, I.K.,Paez-Espino, D.,Kyrpides, N.C.,Yoshikuni, Y.,McDermott, J.E.,Hofmockel, K.S.,Cort, J.R.,Jansson, J.K.
Structural characterization of a soil viral auxiliary metabolic gene product - a functional chitosanase.
Nat Commun, 13:5485-5485, 2022
Cited by
PubMed Abstract: Metagenomics is unearthing the previously hidden world of soil viruses. Many soil viral sequences in metagenomes contain putative auxiliary metabolic genes (AMGs) that are not associated with viral replication. Here, we establish that AMGs on soil viruses actually produce functional, active proteins. We focus on AMGs that potentially encode chitosanase enzymes that metabolize chitin - a common carbon polymer. We express and functionally screen several chitosanase genes identified from environmental metagenomes. One expressed protein showing endo-chitosanase activity (V-Csn) is crystalized and structurally characterized at ultra-high resolution, thus representing the structure of a soil viral AMG product. This structure provides details about the active site, and together with structure models determined using AlphaFold, facilitates understanding of substrate specificity and enzyme mechanism. Our findings support the hypothesis that soil viruses contribute auxiliary functions to their hosts.
PubMed: 36123347
DOI: 10.1038/s41467-022-32993-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.3 Å)
Structure validation

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