In:
Acta Crystallographica Section D Biological Crystallography, International Union of Crystallography (IUCr), Vol. 70, No. 11 ( 2014-11-01), p. 2800-2812
Abstract:
Helicobacter pylori infection causes a variety of gastrointestinal diseases, including peptic ulcers and gastric cancer. Its colonization of the gastric mucosa of the human stomach is a prerequisite for survival in the stomach. Colonization depends on its motility, which is facilitated by the helical shape of the bacterium. In H. pylori , cross-linking relaxation or trimming of peptidoglycan muropeptides affects the helical cell shape. Csd4 has been identified as one of the cell shape-determining peptidoglycan hydrolases in H. pylori . It is a Zn 2+ -dependent D,L-carboxypeptidase that cleaves the bond between the γ-D-Glu and the m DAP of the non-cross-linked muramyltripeptide (muramyl-L-Ala-γ-D-Glu- m DAP) of the peptidoglycan to produce the muramyldipeptide (muramyl-L-Ala-γ-D-Glu) and m DAP. Here, the crystal structure of H. pylori Csd4 (HP1075 in strain 26695) is reported in three different states: the ligand-unbound form, the substrate-bound form and the product-bound form. H. pylori Csd4 consists of three domains: an N-terminal D,L-carboxypeptidase domain with a typical carboxypeptidase fold, a central β-barrel domain with a novel fold and a C-terminal immunoglobulin-like domain. The D,L-carboxypeptidase domain recognizes the substrate by interacting primarily with the terminal m DAP moiety of the muramyltripeptide. It undergoes a significant structural change upon binding either m DAP or the m DAP-containing muramyltripeptide. It it also shown that Csd5, another cell-shape determinant in H. pylori , is capable of interacting not only with H. pylori Csd4 but also with the dipeptide product of the reaction catalyzed by Csd4.
Type of Medium:
Online Resource
ISSN:
1399-0047
DOI:
10.1107/S1399004714018732
DOI:
10.1107/S1399004714018732/mh5144sup1.pdf
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2014
detail.hit.zdb_id:
2020492-9
detail.hit.zdb_id:
2968623-4
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