Noncollagenous region of the streptococcal collagen-like protein is a trimerization domain that supports refolding of adjacent homologous and heterologous collagenous domains.
Noncollagenous region of the streptococcal collagen-like protein is a trimerization domain that supports refolding of adjacent homologous and heterologous collagenous domains.
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链球菌胶原蛋白样蛋白的非胶原区域是一个三聚化结构域，支持相邻同源和异源胶原结构域的重折叠。
DOI：
10.1002/pro.356
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发表时间：
2010
期刊：
影响因子：
--
通讯作者：
Inouye,Masayori
中科院分区：
文献类型：
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作者：
Yu,Zhuoxin;Mirochnitchenko,Oleg;Xu,Chunying;Yoshizumi,Ayumi;Brodsky,Barbara;Inouye,Masayori
动物胶原蛋白的(Gly-Xaa-Yaa)n序列的正确折叠需要相邻的N-端或C-端非胶原性三聚结构域，这些结构域通常包含卷曲的卷曲或β-折叠结构。最近在一些细菌中发现了类胶原蛋白，但对其折叠机制知之甚少。化脓性链球菌的Scl2胶原样蛋白具有一个N端球状结构域，命名为VSP，与其三螺旋结构域相邻。Vsp域是Scl2蛋白在体外正确折叠所必需的。在这里，重组Vsp域单独形成具有显著α-螺旋含量的三聚体，并且具有Tm=45°C的热稳定性。对新构建物的检测表明，只有当Vsp域的N端位于三螺旋结构域的N端时，才能促进体外折叠的效率，而当C端位于三螺旋结构域的N端时，Vsp结构域不能促进体外折叠的效率。将Vsp结构域N-末端与产气荚膜梭菌的异源(Gly-Xaa-Yaa)n序列融合，可以正确地折叠和重折叠这个三螺旋结构，而这个三螺旋结构本身不能折叠成三螺旋的可溶性蛋白。这些结果表明，将功能三聚模块放置在异源Gly-Xaa-YaA重复序列旁边，在某些情况下可以导致正确的折叠，但在三聚和三螺旋结构域的相对位置上也显示出特异性。这些关于其模块化性质的信息可用于生产用于生物材料应用的新型细菌胶原。
Proper folding of the (Gly‐Xaa‐Yaa)nsequence of animal collagens requires adjacent N‐ or C‐terminal noncollagenous trimerization domains which often contain coiled‐coil or beta sheet structure. Collagen‐like proteins have been found recently in a number of bacteria, but little is known about their folding mechanism. The Scl2 collagen‐like protein fromStreptococcus pyogeneshas an N‐terminal globular domain, designated Vsp, adjacent to its triple‐helix domain. The Vspdomain is required for proper refolding of the Scl2 proteinin vitro. Here, recombinant Vspdomain alone is shown to form trimers with a significant α‐helix content and to have a thermal stability of Tm= 45°C. Examination of a new construct shows that the Vspdomain facilitates efficientin vitrorefolding only when it is located N‐terminal to the triple‐helix domain but not when C‐terminal to the triple‐helix domain. Fusion of the Vspdomain N‐terminal to a heterologous (Gly‐Xaa‐Yaa)nsequence fromClostridium perfringensled to correct folding and refolding of this triple‐helix, which was unable to fold into a triple‐helical, soluble protein on its own. These results suggest that placement of a functional trimerization module adjacent to a heterologous Gly‐Xaa‐Yaa repeating sequence can lead to proper folding in some cases but also shows specificity in the relative location of the trimerization and triple‐helix domains. This information about their modular nature can be used in the production of novel types of bacterial collagen for biomaterial applications.