A new structural class of bacterial thioester domains reveals a slipknot topology.

A new structural class of bacterial thioester domains reveals a slipknot topology.
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DOI:
10.1002/pro.3478
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发表时间:
2018-09
期刊:
Protein science : a publication of the Protein Society
影响因子:
--
通讯作者:
Schwarz-Linek U
Schwarz-Linek U
中科院分区:
其他
文献类型:
--
作者:
Miller OK;Banfield MJ;Schwarz-Linek U

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在革兰氏阳性细菌中发现的越来越多的表面相关蛋白的特征是结构保守的硫酯、异肽和酯结构域(TIE 蛋白)中的分子内交联。根据序列预测了两类硫酯结构域 (TED),迄今为止,仅对 I 类结构域的代表进行了结构表征。在这里,我们展示了来自炭疽杆菌、耐万古霉素金黄色葡萄球菌和耐万古霉素屎肠球菌的三种 II 类 TED 的晶体结构。这些蛋白质在结构上与 I 类 TED 不同,因为 β 夹心结构域插入到保守的 TED 折叠中形成活结结构。此外,炭疽芽孢杆菌 TED 结构域是在全长分选酶锚定蛋白结构 (BaTIE) 的背景下呈现的。这提供了对 TIE 蛋白三维排列的深入了解,TIE 蛋白是革兰氏阳性细菌中非常丰富的假定粘附素。
An increasing number of surface‐associated proteins identified in Gram‐positive bacteria are characterized by intramolecular cross‐links in structurally conserved thioester, isopeptide, and ester domains (TIE proteins). Two classes of thioester domains (TEDs) have been predicted based on sequence with, to date, only representatives of Class I structurally characterized. Here, we present crystal structures of three Class II TEDs from Bacillus anthracis, vancomycin‐resistant Staphylococcus aureus, and vancomycin‐resistant Enterococcus faecium. These proteins are structurally distinct from Class I TEDs due to a β‐sandwich domain that is inserted into the conserved TED fold to form a slipknot structure. Further, the B. anthracis TED domain is presented in the context of a full‐length sortase‐anchored protein structure (BaTIE). This provides insight into the three‐dimensional arrangement of TIE proteins, which emerge as very abundant putative adhesins of Gram‐positive bacteria.
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