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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A 1.2-A snapshot of the final step of bacterial cell wall biosynthesis
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A 1.2-A snapshot of the final step of bacterial cell wall biosynthesis

机译：细菌细胞壁生物合成最后一步的1.2-A快照

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摘要

The cell wall imparts structural strength and shape to bacteria. It is made up of polymeric glycan chains with peptide branches that are cross-linked to form the cell wall. The cross-linking reaction, cat- alyzed by transpeptidases, is the last step in cell wall biosynthesis. These enzymes are members of the family of penicillin-binding proteins, the targets of β-lactam antibiotics. We report herein the structure of a penicillin-binding protein complexed with a cepha- losporin designed to probe the mechanism of the cross-linking reaction catalyzed by transpeptidases. The 1.2-A resolution x-ray structure of this cephalosporin bound to the active site of the bifunctional serine type D-alanyl-D-alanine carboxypeptidase/ transpeptidase (EC 3.4.16.4) from Streptomyces SP. strain R61 reveals how the two peptide strands from the polymeric substrates are sequestered in the active site of a transpeptidase. The structure 0f this complex provides a snapshot of the enzyme and the bound cell wall components poised for the final and critical cross-linking step of cell wall biosynthesis.
机译：细胞壁赋予细菌结构强度和形状。它由具有链交联以形成细胞壁的肽分支的聚合聚糖链组成。转肽酶催化的交联反应是细胞壁生物合成的最后一步。这些酶是青霉素结合蛋白家族（β-内酰胺类抗生素的靶标）的成员。我们在此报道了与头孢菌素复合的青霉素结合蛋白的结构，该结构旨在探测转肽酶催化的交联反应的机理。该头孢菌素的1.2-A分辨率X射线结构与链霉菌SP的双功能丝氨酸D-丙氨酸-D-丙氨酸羧肽酶/转肽酶（EC 3.4.16.4）的活性位点结合。菌株R61揭示了如何将来自聚合物底物的两条肽链隔离在转肽酶的活性位点中。该复合物的结构0f提供了酶和结合的细胞壁成分的快照，用于细胞壁生物合成的最终和关键交联步骤。

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