7tpu
From Proteopedia
Crystal structure of a chitinase-modifying protein from Fusarium vanettenii (Fvan-cmp)
Structural highlights
FunctionPGH_FUSV7 Serine-type endopeptidase that cleaves Gly-Gly bonds in the polyglycine linker of host plant class IV chitinases to disrupt their chitin-binding, and thereby plays a role in lowering the defense responses of the host to the fungus (PubMed:36762862). Degrades Z.mays Endochitinase A (CHIA) in vitro, although corn is not its host species (PubMed:35240278, PubMed:36762862).[1] [2] Publication Abstract from PubMedPolyglycine hydrolases (PGHs) are secreted fungal proteases that cleave the polyglycine linker of Zea mays ChitA, a defensive chitinase, thus overcoming one mechanism of plant resistance to infection. Despite their importance in agriculture, there has been no previous structural characterization of this family of proteases. The objective of this research was to investigate the proteolytic mechanism and other characteristics by structural and biochemical means. Here, the first atomic structure of a polyglycine hydrolase was identified. It was solved by X-ray crystallography using a RoseTTAFold model, taking advantage of recent technical advances in structure prediction. PGHs are composed of two domains: the N- and C-domains. The N-domain is a novel tertiary fold with an as-yet unknown function that is found across all kingdoms of life. The C-domain shares structural similarities with class C beta-lactamases, including a common catalytic nucleophilic serine. In addition to insights into the PGH family and its relationship to beta-lactamases, the results demonstrate the power of complementing experimental structure determination with new computational techniques. Crystal structure of a polyglycine hydrolase determined using a RoseTTAFold model.,Dowling NV, Naumann TA, Price NPJ, Rose DR Acta Crystallogr D Struct Biol. 2023 Feb 1;79(Pt 2):168-176. doi: , 10.1107/S2059798323000311. Epub 2023 Feb 6. PMID:36762862[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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