Schacherl, Magdalena ORCID: 0000-0002-5478-2509, Pichlo, Christian, Neundorf, Ines ORCID: 0000-0001-6450-3991 and Baumann, Ulrich (2015). Structural Basis of Proline-Proline Peptide Bond Specificity of the Metalloprotease Zmp1 Implicated in Motility of Clostridium difficile. Structure, 23 (9). S. 1632 - 1643. CAMBRIDGE: CELL PRESS. ISSN 1878-4186

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Abstract

Clostridium difficile is a pathogenic bacterium causing gastrointestinal diseases from mild diarrhea to toxic megacolon. In common with other pathogenic bacteria, C. difficile secretes proteins involved in adhesion, colonization, and dissemination. The recently identified Zmp1 is an extracellular metalloprotease showing a unique specificity for Pro-Pro peptide bonds. The endogenous substrates of Zmp1 are two surface proteins implicated in adhesion of C. difficile to surface proteins of human cells. Thus, Zmp1 is believed to be involved in the regulation of the adhesion-motility balance of C. difficile. Here, we report crystal structures of Zmp1 from C. difficile in its unbound and peptide-bound forms. The structure analysis revealed a fold similar to Bacillus anthracis lethal factor. Crystal structures in the open and closed conformation of the S-loop shed light on the mode of binding of the substrate, and reveal important residues for substrate recognition and the strict specificity of Zmp1 for Pro-Pro peptide bonds.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Schacherl, MagdalenaUNSPECIFIEDorcid.org/0000-0002-5478-2509UNSPECIFIED
Pichlo, ChristianUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Neundorf, InesUNSPECIFIEDorcid.org/0000-0001-6450-3991UNSPECIFIED
Baumann, UlrichUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
URN: urn:nbn:de:hbz:38-394405
DOI: 10.1016/j.str.2015.06.018
Journal or Publication Title: Structure
Volume: 23
Number: 9
Page Range: S. 1632 - 1643
Date: 2015
Publisher: CELL PRESS
Place of Publication: CAMBRIDGE
ISSN: 1878-4186
Language: English
Faculty: Faculty of Mathematics and Natural Sciences
Divisions: Faculty of Mathematics and Natural Sciences > Department of Chemistry > Institute of Biochemistry
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
LETHAL FACTOR; PROTEOLYTIC-ENZYMES; BACILLUS-ANTHRACIS; CRYSTAL-STRUCTURE; KINASE-KINASE; EF-P; TOXIN; PROTEASE; IDENTIFICATION; VALIDATIONMultiple languages
Biochemistry & Molecular Biology; Biophysics; Cell BiologyMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/39440

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