Purification, crystallization and preliminary X-ray crystallographic analysis of the UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D- alanine ligase (MurF) from Acinetobacter baumannii SCIE SCOPUS

Cited 3 time in WEB OF SCIENCE Cited 3 time in Scopus
Title
Purification, crystallization and preliminary X-ray crystallographic analysis of the UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D- alanine ligase (MurF) from Acinetobacter baumannii
Author(s)
An, Young Jun; Jeong, Chang-Sook; Yu, Jeong Hee; Chung, Kyung Min; Cha, Sun-Shin
KIOST Author(s)
An, Young Jun(안영준)
Alternative Author(s)
안영준; 정창숙; 차선신
Publication Year
2014-07
Abstract
The emergence and global spread of multidrug-resistant Acinetobacter baumannii strains are major threats to public health. Inhibition of peptidoglycan biosynthesis is an effective strategy for the development of antibiotics. The ATP-dependent UDP-N-acetylmuramoyl-tripeptide-d-alanyl-d-alanine ligase (MurF) that is responsible for the last step of peptidoglycan biosynthesis is a validated target for the development of antibiotics. Crystals of A. baumannii MurF in complex with ATP were grown by the microbatch crystallization method at 295 K. The crystals belonged to space group P3221, with unit-cell parameters a = b = 85.42, c = 129.86 angstrom. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 54.32%.
ISSN
1744-3091
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/2778
DOI
10.1107/S2053230X14009984
Bibliographic Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.70, pp.976 - 978, 2014
Publisher
INT UNION CRYSTALLOGRAPHY
Keywords
Acinetobacter baumannii; MurF
Type
Article
Language
English
Document Type
Article
Publisher
INT UNION CRYSTALLOGRAPHY
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