期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 381, 期 1, 页码 16-21出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.01.186
关键词
Sphingomonas; Peptidoglycan; Glycoside hydrolase; FlgJ; Crystal structure
资金
- Japan Synchrotron Radiation Research Institute (JASRI) [BL38B1]
- Targeted Proteins Research Program
- Ministry of Education, Culture, Sports, Science, and Technology (MEXT) of Japan
- Showa Houkoukai Foundation
Glycoside hydrolase (GH) categorized into family 73 plays an important role in degrading bacterial cell wall peptidoglycan. The flagellar protein FlgJ contains N- and C-terminal domains responsible for flagellar rod assembly and peptidoglycan hydrolysis, respectively. A member of family GH-73, the C-terminal domain (SPH1045-C) of FlgJ from Sphingomonas sp. strain A1 was expressed in Escherichia coli, purified, and characterized. SPH1045-C exhibited bacterial cell lytic activity most efficiently at pH 6.0 and 37 degrees C. The X-ray crystallographic structure of SPH1045-C was determined at 1.74 angstrom resolution by single-wavelength anomalous diffraction. The enzyme consists of two lobes, a and p. A deep cleft located between the two lobes can accommodate polymer molecules, suggesting that the active site is located in the cleft. Although SPH1045-C shows a structural homology with family GH-22 and GH-23 lysozymes, the arrangement of the nucleophile/base residue in the active site is specific to each peptidoglycan hydrolase. (C) 2009 Elsevier Inc. All rights reserved.
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