Solution Structure of IseA, an Inhibitor Protein of dl-Endopeptidases from Bacillus subtilis, Reveals a Novel Fold with a Characteristic Inhibitory Loop-Reference-Cited by-同舟云学术

Solution Structure of IseA, an Inhibitor Protein of dl-Endopeptidases from Bacillus subtilis, Reveals a Novel Fold with a Characteristic Inhibitory Loop

Published:2012-12 Issue:53 Volume:287 Page:44736-44748
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Arai Ryoichi,Fukui Sadaharu,Kobayashi Naoya,Sekiguchi Junichi

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference61 articles.

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4. Regulation of a new cell wall hydrolase gene, cwlF, which affects cell separation in Bacillus subtilis;Ishikawa;J. Bacteriol.,1998

5. Peptidoglycan hydrolase LytF plays a role in cell separation with CwlF during vegetative growth of Bacillus subtilis;Ohnishi;J. Bacteriol.,1999

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