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首页> 外文期刊>Journal of structural and functional genomics >Novel hexamerization motif is discovered in a conserved cytoplasmic protein from Salmonella typhimurium
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Novel hexamerization motif is discovered in a conserved cytoplasmic protein from Salmonella typhimurium

机译：在鼠伤寒沙门氏菌的保守胞质蛋白中发现了新的六聚体基序

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摘要

The cytoplasmic protein Stm3548 of unknown function obtained from a strain of Salmonella typhimurium was determined by X-ray crystallography at a resolution of 2.25??. The asymmetric unit contains a hexamer of structurally identical monomers. The monomer is a globular domain with a long β-hairpin protrusion that distinguishes this structure. This β-hairpin occupies a central position in the hexamer, and its residues participate in the majority of interactions between subunits of the hexamer. We suggest that the structure of Stm3548 presents a new hexamerization motif. Because the residues participating in interdomain interactions are highly conserved among close members of protein family DUF1355 and buried solvent accessible area for the hexamer is significant, the hexamer is most likely conserved as well. A light scattering experiment confirmed the presence of hexamer in solution.
机译：通过X-射线晶体学以2.25 -6的分辨率测定从鼠伤寒沙门氏菌菌株获得的功能未知的胞质蛋白Stm3548。不对称单元包含结构相同单体的六聚体。该单体是具有长β-发夹突出物的球状结构域，可以区分该结构。该β-发夹在六聚体中占据中心位置，并且其残基参与六聚体的亚基之间的大多数相互作用。我们建议Stm3548的结构提出了一个新的六聚体基序。由于参与域间相互作用的残基在蛋白质家族DUF1355的紧密成员之间是高度保守的，六聚体的掩埋溶剂可及区域非常重要，因此六聚体也很可能是保守的。光散射实验证实溶液中存在六聚体。

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