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Structure of a thermostable serralysin from Serratia sp. FS14 at 1.1 Å resolution
Author(s) -
Wu Dongxia,
Ran Tinting,
Wang Weiwu,
Xu Dongqing
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15023092
Subject(s) - thermostability , serratia , hydrogen bond , crystal structure , stereochemistry , chemistry , crystallography , hydrolase , transferase , resolution (logic) , biology , biochemistry , molecule , enzyme , organic chemistry , pseudomonas , genetics , artificial intelligence , bacteria , computer science
Serralysin 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 Å resolution. Similar to its homologues, it mainly consists of two domains: an N‐terminal catalytic domain and a `parallel β‐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 3 10 ‐helix protruding further from the molecular surface, and that the β‐sheets comprising the `parallel β‐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.

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