Crystal structures of D-alanine-D-alanine ligase from Xanthomonas oryzae pv. oryzae alone and in complex with nucleotides SCIE SCOPUS

Cited 10 time in WEB OF SCIENCE Cited 10 time in Scopus
Title
Crystal structures of D-alanine-D-alanine ligase from Xanthomonas oryzae pv. oryzae alone and in complex with nucleotides
Author(s)
Thanh Thi Ngoc Doan; Kim, Jin-Kwang; Ho-Phuong-Thuy Ngo; Huyen-Thi Tran; Cha, Sun-Shin; Chung, Kyung Min; Huynh, Kim-Hung; Ahn, Yeh-Jin; Kang, Lin-Woo
Publication Year
2014-03-01
Abstract
D-Alanine-D-alanine ligase (DDL) catalyzes the biosynthesis of D-alanyl-D-alanine, an essential bacterial peptidoglycan precursor, and is an important drug target for the development of antibacterials. We determined four different crystal structures of DDL from Xanthomonas oryzae pv. myzae (Xoo) causing Bacteria Blight (BB), which include apo, ADP-bound, ATP-bound, and AMPPNP-bound structures at the resolution between 2.3 and 2.0 angstrom. Similarly with other DDLs, the active site of XoDDL is formed by three loops from three domains at the center of enzyme. Compared with D-alanyl-D-alanine and ATP-bound TtDDL structure, the gamma-phosphate of ATP in XoDDL structure was shifted outside toward solution. We swapped the omega-loop (loop3) of XoDDL with those of Escherichia coli and Helicobacter pylori DDLs, and measured the enzymatic kinetics of wild-type XoDDL and two mutant XoDDLs with the swapped omega-loops. Results showed that the direct interactions between omega-loop and other two loops are essential for the active ATP conformation for D-ala-phosphate formation. (C) 2014 Elsevier Inc. All rights reserved.
ISSN
0003-9861
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/2892
DOI
10.1016/j.abb.2014.01.009
Bibliographic Citation
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, v.545, pp.92 - 99, 2014
Publisher
ELSEVIER SCIENCE INC
Subject
CYSTATHIONINE BETA-LYASE; ALANYL-D-ALANINE; ESCHERICHIA-COLI; CRYSTALLIZATION; PHOSPHATE; REFMAC5
Keywords
D-Alanine-D-alanine ligase (DDL); Drug target; Bacterial cell wall synthesis; Xanthomonas oryzae pv. oryzae (Xoo); X-ray crystallography
Type
Article
Language
English
Document Type
Article
Publisher
ELSEVIER SCIENCE INC
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