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Structural basis for the recognition of muramyltripeptide byHelicobacter pyloriCsd4, a<scp>D</scp>,<scp>L</scp>-carboxypeptidase controlling the helical cell shape
- Source :
- Acta Crystallographica Section D: Biological Crystallography
- Publication Year :
- 2014
- Publisher :
- International Union of Crystallography (IUCr), 2014.
-
Abstract
- H. pylori Csd4 (HP1075), together with other peptidoglycan hydrolases, plays an important role in determining the helical cell shape. Its crystal structure has been determined in three different forms.<br />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 Zn2+-dependent d,l-carboxypeptidase that cleaves the bond between the γ-d-Glu and the mDAP of the non-cross-linked muramyl­tripeptide (muramyl-l-Ala-γ-d-Glu-mDAP) of the peptidoglycan to produce the muramyldipeptide (muramyl-l-Ala-γ-d-Glu) and mDAP. 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 mDAP moiety of the muramyltripeptide. It undergoes a significant structural change upon binding either mDAP or the mDAP-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.
- Subjects :
- Models, Molecular
meso-diaminopimelate
Protein Conformation
Molecular Sequence Data
pgp1
csd4
csd5
Carboxypeptidases
Plasma protein binding
peptidoglycan
Crystallography, X-Ray
cell shape
Helicobacter Infections
chemistry.chemical_compound
Protein structure
Bacterial Proteins
Structural Biology
Hydrolase
d,l-carboxypeptidase
Humans
Amino Acid Sequence
Binding site
Peptide sequence
Binding Sites
Helicobacter pylori
biology
General Medicine
biology.organism_classification
Research Papers
Carboxypeptidase
Protein Structure, Tertiary
3. Good health
chemistry
Biochemistry
Muramic Acids
biology.protein
Peptidoglycan
HP1075
Oligopeptides
Sequence Alignment
Protein Binding
Subjects
Details
- ISSN :
- 13990047
- Volume :
- 70
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section D Biological Crystallography
- Accession number :
- edsair.doi.dedup.....33f6204297a730126953e2a7431abcce