Catalysis of protein folding by chaperones in pathogenic bacteria
Catalysis of protein folding by chaperones in pathogenic bacteria
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DOI：
10.1073/pnas.0408072101
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发表时间：
2004-12-14
影响因子：
11.1
通讯作者：
Hultgren, SJ
中科院分区：
文献类型：
--
作者：
Bann, JG;Pinkner, JS;Hultgren, SJ
分子伴侣被认为可以抑制聚集等非途径相互作用的发生，而不会影响天然结构的途径上形成。在这里，我们提出了一种机制，其中家族的PapD样分子伴侣，这是参与形成的粘附性皮利在致病菌，功能抑制聚集，同时催化折叠的亚基，使菌毛。我们还表明，Arg-8残基，不变的裂缝中的所有已知的PapD样分子伴侣，组成的分子伴侣的活性位点的一部分。数据认为，催化折叠的时间机制。菌毛亚基的末端羧酸基团通过氢键结合锚定到分子伴侣的活性位点。这种键合在空间上将亚基的COOH末端固定在β折叠形成的正确上下文中，使用分子伴侣的NH 2末端结构域的边缘作为成核位点。
Molecular chaperones are thought to inhibit off-pathway interactions such as aggregation from occurring without influencing the on-pathway formation of native structure. Here, we present a mechanism whereby the family of PapD-like chaperones, which are involved in the formation of adhesive pili in pathogenic bacteria, function by suppressing aggregation while simultaneously catalyzing the folding of subunits that make up the pilus. We also show that the Arg-8 residue, invariant in the cleft of all known PapD-like chaperones, makes up part of the active site of the chaperone. The data argue for a temporal mechanism of catalyzed folding. The terminal carboxylate group of a pilus subunit anchors to the active site of the chaperone by hydrogen bonding. This bonding spatially fixes the COOH terminus of the subunit in the correct context for beta-sheet formation, using the edge of the NH2-terminal domain of the chaperone as a nucleation site.