1.8 Å resolution crystal structure of the carbapenem intrinsic resistance protein CarF

被引：1

作者：

Tichy, Evelyn M. ^{[1
]}

Hardwick, Steven W. ^{[1
]}

Luisi, Ben F. ^{[1
]}

Salmond, George P. C. ^{[1
]}

机构：

[1] Univ Cambridge, Dept Biochem, Bldg O,Downing Site, Cambridge CB2 1QW, England

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2017年 / 73卷

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

antibiotic resistance; carbapenem; intrinsic resistance; CIR family; CLec domain; ANTIBIOTIC PRODUCTION GENES; BETA-LACTAM BIOSYNTHESIS; ERWINIA-CAROTOVORA; ENTEROBACTER-AEROGENES; STRUCTURE PREDICTION; IMIPENEM RESISTANCE; SERRATIA; BACTERIA; SERVER; IDENTIFICATION;

D O I：

10.1107/S2059798317002236

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The natural production of the beta-lactam antibiotic carbapenem in bacteria involves a group of enzymes that form a synthetic pathway as well as proteins that protect the cell from self-intoxification by the products. Here, the crystal structure of CarF, one of the two proteins that confer resistance to synthesis of the antibiotic in the host organism, is reported. The CarF fold places it within a widely occurring structural family, indicating an ancient structural origin from which the resistance function has been derived.

引用

页码：549 / 556

页数：8

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