Structure of a thermostable serralysin from Serratia sp FS14 at 1.1Å resolution
Structure of a thermostable serralysin from Serratia sp FS14 at 1.1Å resolution
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来自 Serratia sp FS14 的热稳定性 serralysin 的结构，分辨率为 1.1 埃
DOI：
10.1107/s2053230x15023092
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发表时间：
2016-01-01
影响因子：
0.9
通讯作者：
Xu, Dongqing
中科院分区：
文献类型：
--
作者：
Wu, Dongxia;Ran, Tinting;Xu, Dongqing
seralysin是一种被充分研究的金属蛋白酶，典型的seralysin不耐热。从Serratia sp. FS14中分离得到的serralysin具有热稳定性，为了揭示其热稳定性的机制，在1.10埃分辨率下对Serratia sp. FS14中serralysin的晶体结构进行了解析，晶体学R因子为0.1619。与其同系物类似，它主要由两个结构域组成：n端催化结构域和“平行β -roll”c端结构域。比较研究表明，由于189-198环，催化活性位点空腔的形状更加开放，短的3（10）螺旋从分子表面进一步突出，并且包含“平行β -滚”的β -片比其同系物更长。其中一个非保守残基（Asn200）与Lys27形成氢键可能有助于热稳定性。
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 angstrom 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 3(10)-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.