• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Crystal structures of an oligopeptide-binding protein from the biosynthetic pathway of the beta-lactamase inhibitor clavulanic acid.
【24h】

Crystal structures of an oligopeptide-binding protein from the biosynthetic pathway of the beta-lactamase inhibitor clavulanic acid.

机译：来自β-内酰胺酶抑制剂克拉维酸的生物合成途径的寡肽结合蛋白的晶体结构。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Clavulanic acid (CA) is a clinically important beta-lactamase inhibitor that is produced by fermentation of Streptomyces clavuligerus. The CA biosynthesis pathway starts from arginine and glyceraldehyde-3-phosphate and proceeds via (3S,5S)-clavaminic acid, which is converted to (3R,5R)-clavaldehyde, the immediate precursor of (3R,5R)-CA. Open reading frames 7 (orf7) and 15 (orf15) of the CA biosynthesis cluster encode oligopeptide-binding proteins (OppA1 and OppA2), which are essential for CA biosynthesis. OppA1/2 are proposed to be involved in the binding and/or transport of peptides across the S. clavuligerus cell membrane. Peptide binding assays reveal that recombinant OppA1 and OppA2 bind di-/tripeptides containing arginine and certain nonapeptides including bradykinin. Crystal structures of OppA2 in its apo form and in complex with arginine or bradykinin were solved to 1.45, 1.7, and 1.7 A resolution, respectively. The overall fold of OppA2 consists of two lobes with a deep cavity in the center, as observed for other oligopeptide-binding proteins. The large cavity creates a peptide/arginine binding cleft. The crystal structures of OppA2 in complex with arginine or bradykinin reveal that the C-terminal arginine of bradykinin binds similarly to arginine. The results are discussed in terms of the possible roles of OppA1/2 in CA biosynthesis.
机译：棒酸（CA）是临床上重要的β-内酰胺酶抑制剂，可通过发酵链霉菌产生。 CA的生物合成途径从精氨酸和3-磷酸甘油醛开始，并通过（3S，5S）-克拉维酸进行，然后转化为（3R，5R）-克拉醛，即（3R，5R）-CA的直接前体。 CA生物合成簇的开放阅读框7（orf7）和15（orf15）编码寡肽结合蛋白（OppA1和OppA2），这对于CA生物合成至关重要。提议OppA1 / 2参与跨锁骨链霉菌细胞膜的肽的结合和/或转运。肽结合测定法揭示重组OppA1和OppA2结合含有精氨酸和某些非肽（包括缓激肽）的二肽/三肽。 OppA2的载脂蛋白形式以及与精氨酸或缓激肽复合的晶体结构分别解析为1.45 A，1.7 A和1.7 A分辨率。正如其他寡肽结合蛋白所观察到的那样，OppA2的整体折叠由两个叶瓣组成，两个叶瓣的中心都有一个深洞。大腔产生肽/精氨酸结合裂隙。 OppA2与精氨酸或缓激肽复合的晶体结构表明，缓激肽的C末端精氨酸与精氨酸的结合相似。根据OppA1 / 2在CA生物合成中的可能作用来讨论结果。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号