Crystallization and preliminary X-ray analysis of a d-alanyl-d-alanine ligase (EcDdlB) from Escherichia coli

被引：7
作者：
Batson, Sarah [1 ]
Rea, Dean [1 ]
Fulop, Vilmos [1 ]
Roper, David I. [1 ]
机构：
[1] Univ Warwick, Dept Biol Sci, Coventry CV4 7AL, W Midlands, England
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
基金：
英国惠康基金;
关键词：
peptidoglycans; d-alanyl-d-alanine ligase; DdlB; D-LACTATE LIGASE; VANCOMYCIN RESISTANCE; CRYSTAL-STRUCTURE; ACTIVE-SITE; DDLA GENE; PURIFICATION; SYNTHETASE; VANA; ENTEROCOCCI; INHIBITION;
D O I：
10.1107/S1744309110003970
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
A recombinant form of Escherichia coli DdlB (EcDdlB) has been prepared and cocrystallized with ADP and d-alanyl-d-alanine to represent the ternary complex of EcDdlB. Furthermore, EcDdlB has been cocrystallized under the same conditions with the ligands ATP and d-alanyl-d-alanine, representing the product-inhibited complex. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.0, b = 97.6, c = 109.5 A and a = 51.2, b = 97.8, c = 110.1 A, respectively, and both contained two molecules in the asymmetric unit. Complete data sets were collected to 1.5 and 1.4 A resolution, respectively, from single crystals under cryogenic conditions using synchrotron radiation.
引用
收藏
页码：405 / 408
页数：4
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