5d7w
From Proteopedia
Crystal structure of serralysin
Structural highlights
FunctionPRZN_SERMA Has insecticidal activity against the locust M.palpalis. When administered orally to locusts at a low dose it causes them to lie on their sides exhibiting sporadic limb movements and muscular twitching, followed by full recovery. When administered at higher doses the same symptoms are observed, followed by death. Publication Abstract from PubMedSerralysin is a well studied metalloprotease, and typical serralysins are not thermostable. The serralysin isolated from Serratia sp. FS14 was found to be thermostable, and in order to reveal the mechanism responsible for its thermostability, the crystal structure of serralysin from Serratia sp. FS14 was solved to a crystallographic R factor of 0.1619 at 1.10 A resolution. Similar to its homologues, it mainly consists of two domains: an N-terminal catalytic domain and a `parallel beta-roll' C-terminal domain. Comparative studies show that the shape of the catalytic active-site cavity is more open owing to the 189-198 loop, with a short 310-helix protruding further from the molecular surface, and that the beta-sheets comprising the `parallel beta-roll' are longer than those in its homologues. The formation of hydrogen bonds from one of the nonconserved residues (Asn200) to Lys27 may contribute to the thermostability. Structure of a thermostable serralysin from Serratia sp. FS14 at 1.1 A resolution.,Wu D, Ran T, Wang W, Xu D Acta Crystallogr F Struct Biol Commun. 2016 Jan;72(Pt 1):10-5. doi:, 10.1107/S2053230X15023092. Epub 2016 Jan 1. PMID:26750478[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Serratia marcescens | Ran T | Wang W | Wu D | Xu DQ
