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首页> 外文期刊>Acta crystallographica, Section D. Biological crystallography >Structure of Csd3 from Helicobacter pylori, a cell shape-determining metallopeptidase
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Structure of Csd3 from Helicobacter pylori, a cell shape-determining metallopeptidase

机译：幽门螺杆菌Csd3的结构，一种确定细胞形状的金属肽酶

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摘要

Helicobacter pylori is associated with various gastrointestinal diseases such as gastritis, ulcers and gastric cancer. Its colonization of the human gastric mucosa requires high motility, which depends on its helical cell shape. Seven cell shape-determining genes (csd1, csd2, csd3/hdpA, ccmA, csd4, csd5 and csd6) have been identified in H. pylori. Their proteins play key roles in determining the cell shape through modifications of the cell-wall peptidoglycan by the alteration of cross-linking or by the trimming of peptidoglycan muropeptides. Among them, Csd3 (also known as HdpA) is a bifunctional enzyme. Its D,D-endopeptidase activity cleaves the D-Ala(4)-mDAP(3) peptide bond between cross-linked muramyl tetrapeptides and pentapeptides. It is also a D,D-carboxypeptidase that cleaves off the terminal D-Ala 5 from the muramyl pentapeptide. Here, the crystal structure of this protein has been determined, revealing the organization of its three domains in a latent and inactive state. The N-terminal domain 1 and the core of domain 2 share the same fold despite a very low level of sequence identity, and their surface-charge distributions are different. The C-terminal LytM domain contains the catalytic site with a Zn2+ ion, like the similar domains of other M23 metallopeptidases. Domain 1 occludes the active site of the LytM domain. The core of domain 2 is held against the LytM domain by the C-terminal tail region that protrudes from the LytM domain.
机译：幽门螺杆菌与各种胃肠道疾病如胃炎，溃疡和胃癌有关。其在人胃粘膜上的定殖需要高动力，这取决于其螺旋细胞的形状。在幽门螺杆菌中已鉴定出七个确定细胞形状的基因（csd1，csd2，csd3 / hdpA，ccmA，csd4，csd5和csd6）。它们的蛋白质在通过改变交联键或修整肽聚糖多肽而修饰细胞壁肽聚糖的过程中，在决定细胞形状中起关键作用。其中，Csd3（也称为HdpA）是一种双功能酶。它的D，D-内肽酶活性可切割交联的ram基四肽和五肽之间的D-Ala（4）-mDAP（3）肽键。这也是一种D，D-羧肽酶，其从所述戊二酰五肽中切割出末端D-Ala 5。在这里，已经确定了该蛋白质的晶体结构，揭示了其三个结构域在潜伏和无活性状态下的组织。尽管序列同一性水平很低，但N末端结构域1和结构域2的核心共享相同的折叠，并且它们的表面电荷分布不同。 C端LytM结构域包含带有Zn2 +离子的催化位点，就像其他M23金属肽酶的类似结构域一样。域1遮盖了LytM域的活动位点。结构域2的核心通过从LytM结构域突出的C末端尾部区域紧靠LytM结构域。

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