VANCOMYCIN RESISTANCE - STRUCTURE OF D-ALANINE-D-ALANINE LIGASE AT 2.3-ANGSTROM RESOLUTION

被引：243

作者：

FAN, C

MOEWS, PC

WALSH, CT

KNOX, JR

机构：

[1] UNIV CONNECTICUT, DEPT MOLEC & CELL BIOL, STORRS, CT 06269 USA

[2] HARVARD UNIV, SCH MED, DEPT BIOL CHEM & MOLEC PHARMACOL, BOSTON, MA 02115 USA

来源：

SCIENCE | 1994年 / 266卷 / 5184期

关键词：

D O I：

10.1126/science.7939684

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The molecular structure of the D-alanine:D-alanine ligase of the ddlB gene of Escherichia coli, co-crystallized with an S,R-methylphosphinate and adenosine triphosphate, was determined by x-ray diffraction to a resolution of 2.3 angstroms. A catalytic mechanism for the ligation of two D-alanine substrates is proposed in which a helix dipole and a hydrogen-bonded triad of tyrosine, serine, and glutamic acid assist binding and deprotonation steps. From sequence comparison, it is proposed that a different triad exists in a recently discovered D-alanine:D-lactate ligase (VanA) present in vancomycin-resistant enterococci. A molecular mechanism for the altered specificity of VanA is suggested.

引用

页码：439 / 443

页数：5

共 34 条

[1] GENETICS AND MECHANISMS OF GLYCOPEPTIDE RESISTANCE IN ENTEROCOCCI [J].