Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C beta-lactamases AmpC BER and CMY-10

Na Jung-Hyun; Cha Sun-Shin

首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C beta-lactamases AmpC BER and CMY-10

【24h】

Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C beta-lactamases AmpC BER and CMY-10

机译：扩展的衬底结构依据光谱和structure-guided AmpC误码率发现柠檬酸的抑制活性和对C类beta-lactamases AmpC误码率CMY-10

获取原文

获取原文并翻译 | 示例

掌桥外文数据库（机构版） >>

开具论文收录证明 >>

文献代查 >>

页面导航

摘要
著录项
相似文献
相关主题

摘要

AmpC BER is an extended substrate spectrum class C beta-lactamase with a two-amino-acid insertion in the R2 loop compared with AmpC EC2. The crystal structures of AmpC BER (S64A mutant) and AmpC EC2 were determined. Structural comparison of the two proteins revealed that the insertion increases the conformational flexibility of the R2 loop. Two citrate molecules originating from the crystallization solution were observed in the active site of the S64A mutant. One citrate molecule makes extensive interactions with active-site residues that are highly conserved among class C beta-lactamases, whereas the other one is weakly bound. Based on this structural observation, it is demonstrated that citrate, a primary metabolite that is widely used as a food additive, is a competitive inhibitor of two class C beta-lactamases (AmpC BER and CMY-10). Consequently, the data indicate enhancement of the flexibility of the R2 loop as an operative strategy for molecular evolution of extended-spectrum class C beta-lactamases, and also suggest that the citrate scaffold is recognized by the active sites of class C beta-lactamases.

机译：是一个扩展的底物谱类C AmpC误码率beta-lactamase两种氨基酸插入的R2循环而AmpC EC2。结构(S64A突变)和AmpC EC2 AmpC误码率测定。蛋白质显示插入增加R2的构象的灵活性循环。两个来自柠檬酸分子结晶溶液中观察到S64A突变体的活性部位。分子使广泛的相互作用高度保守的活性位点残基在C类beta-lactamases,而另一个一个是弱。观察,它表明,柠檬酸,广泛用作食品的主要代谢物添加剂,是一种竞争性抑制剂两类C beta-lactamases (AmpC BER和CMY-10)。因此,数据显示增强的R2的灵活性作为一个操作循环分子进化的策略extended-spectrum C类beta-lactamases,还表明,柠檬酸脚手架被类C的活跃的网站beta-lactamases。

著录项

来源
《Acta crystallographica. Section D, Structural biology.》 |2016年第8期|976-985|共10页
作者
Na Jung-Hyun; Cha Sun-Shin;
展开▼
作者单位

Ewha Womans Univ, Dept Chem & Nano Sci, Seoul 03760, South Korea;

展开▼
收录信息
原文格式 PDF
正文语种英语
中图分类
关键词
beta-Lactamases; crystal structure; Food additivesPhospholipase C betaBit error rateCompetitive inhibitionCitratesPRKACB protein, humanActive Site;

机译：beta-Lactamases;晶体结构;食物additivesPhospholipase C betaBit错误rateCompetitive inhibitionCitratesPRKACB蛋白质,humanActive网站;

相似文献

外文文献

1. Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C beta-lactamases AmpC BER and CMY-10 [J] . Na Jung-Hyun, Cha Sun-Shin Acta crystallographica. Section F, Structural biology communications . 2016,第8期

机译：AMPC BER扩展基材谱的结构基础，以及柠檬酸盐抑制活性对Cβ-内酰胺AMPC BER和CMY-10的抑制活性的结构基础
2. Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C beta-lactamases AmpC BER and CMY-10 [J] . Na Jung-Hyun, Cha Sun-Shin Acta crystallographica. Section F, Structural biology communications . 2016,第8期

机译：AMPC BER扩展基材谱的结构基础，以及柠檬酸盐抑制活性对Cβ-内酰胺AMPC BER和CMY-10的抑制活性的结构基础

Structural basis for the extended substrate spectrum of AmpC BER and structure-guided discovery of the inhibition activity of citrate against the class C beta-lactamases AmpC BER and CMY-10

摘要

著录项

相似文献

相关主题

期刊订阅