The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel β-roll
The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel β-roll
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DOI：
10.1038/sj.emboj.7600100
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发表时间：
2004-02-25
期刊：
影响因子：
11.4
通讯作者：
Goldman, A
中科院分区：
文献类型：
--
作者：
Nummelin, H;Merckel, MC;Goldman, A
在1.55埃的分辨率下，对大肠结肠炎耶尔森菌O:3血清型耶尔森菌黏附素YadA重组胶原结合域的晶体结构进行了解析。三聚体结构由头部和颈部区域组成，胶原蛋白结合的头部区域是一种新型的九卷左旋平行β卷。在-滚之前，多肽从一个单体环到其他单体，在-滚之后，颈部区域也做同样的事情，从球形头部区域过渡到更窄的茎域。这创造了一个本质上稳定的“锁紧螺母”结构。三聚体形式的YadA是胶原结合所必需的，其表面残基的诱变可以鉴定推定的胶原结合表面。此外，一个新的YadA β -roll结构序列基序被用于鉴定多种人类和植物病原体中可能存在的YadA-head-like结构域。因此，这些结构域可能是细菌避免宿主反应的一种常见策略。
The crystal structure of the recombinant collagen-binding domain of Yersinia adhesin YadA from Yersinia enterocolitica serotype O:3 was solved at 1.55 Angstrom resolution. The trimeric structure is composed of head and neck regions, and the collagen binding head region is a novel nine-coiled left-handed parallel beta-roll. Before the beta-roll, the polypeptide loops from one monomer to the rest, and after the beta-roll the neck region does the same, making the transition from the globular head region to the narrower stalk domain. This creates an intrinsically stable 'lock nut' structure. The trimeric form of YadA is required for collagen binding, and mutagenesis of its surface residues allowed identification of a putative collagen-binding surface. Furthermore, a new structure-sequence motif for YadA beta-roll was used to identify putative YadA-head-like domains in a variety of human and plant pathogens. Such domains may therefore be a common bacterial strategy for avoiding host response.