Structure of the Yersinia pestis tip protein LcrV refined to 1.65 Å resolution
Structure of the Yersinia pestis tip protein LcrV refined to 1.65 Å resolution
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DOI：
10.1107/s1744309113008579
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发表时间：
2013-05-01
影响因子：
0.9
通讯作者：
De Guzman, Roberto N.
中科院分区：
文献类型：
--
作者：
Chaudhury, Sukanya;Battaile, Kevin P.;De Guzman, Roberto N.
人类病原体鼠疫耶尔森氏菌需要III型分泌系统（T3 SS）的组装以获得毒力。T3 SS的结构成分包括一个外部针和一个尖端复合体，该复合体由Y中的LcrV形成。鼠疫在C273 S背景下的LcrV三重突变体（K40 A/D41 A/K42 A）的结构先前已报道为2.2埃分辨率。在此，以1.65埃的更高分辨率报道了在C273 S背景中没有三重突变的LcrV的晶体结构。总的来说，这两种结构是相似的，但也有显着的差异，特别是在三重突变位点附近。精细结构揭示了残基Gly 28-Asn 43的骨架位置的轻微移动，并且在由残基Ile 46-Val 63组成的环区域中显示出电子密度，其在原始结构中是无序的。此外，跨越残基Tyr 77-Gln 95的螺旋转角区采用不同的取向。
The human pathogen Yersinia pestis requires the assembly of the type III secretion system (T3SS) for virulence. The structural component of the T3SS contains an external needle and a tip complex, which is formed by LcrV in Y. pestis. The structure of an LcrV triple mutant (K40A/D41A/K42A) in a C273S background has previously been reported to 2.2 angstrom resolution. Here, the crystal structure of LcrV without the triple mutation in a C273S background is reported at a higher resolution of 1.65 angstrom. Overall the two structures are similar, but there are also notable differences, particularly near the site of the triple mutation. The refined structure revealed a slight shift in the backbone positions of residues Gly28-Asn43 and displayed electron density in the loop region consisting of residues Ile46-Val63, which was disordered in the original structure. In addition, the helical turn region spanning residues Tyr77-Gln95 adopts a different orientation.