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PMID:11777911

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Citation

Luthy, L, Grutter, MG and Mittl, PR (2002) The crystal structure of Helicobacter pylori cysteine-rich protein B reveals a novel fold for a penicillin-binding protein. J. Biol. Chem. 277:10187-93

Abstract

Colonization of the gastric mucosa with the spiral-shaped Gram-negative proteobacterium Helicobacter pylori is probably the most common chronic infection in humans. The genomes of H. pylori strains J99 and 26695 have been completely sequenced. Functional and three-dimensional structural information is available for less than one third of all open reading frames. We investigated the function and three-dimensional structure of a member from a family of cysteine-rich hypothetical proteins that are unique to H. pylori and Campylobacter jejuni. The structure of H. pylori cysteine-rich protein (Hcp) B possesses a modular architecture consisting of four alpha/alpha-motifs that are cross-linked by disulfide bridges. The Hcp repeat is similar to the tetratricopeptide repeat, which is frequently found in protein/protein interactions. In contrast to the tetratricopeptide repeat, the Hcp repeat is 36 amino acids long. HcpB is capable of binding and hydrolyzing 6-amino penicillinic acid and 7-amino cephalosporanic acid derivatives. The HcpB fold is distinct from the fold of any known penicillin-binding protein, indicating that the Hcp proteins comprise a new family of penicillin-binding proteins. The putative penicillin binding site is located in an amphipathic groove on the concave side of the molecule.

Links

PubMed Online version:10.1074/jbc.M108993200

Keywords

Amino Acid Motifs; Amino Acid Sequence; Amino Acids/chemistry; Bacterial Proteins; Binding Sites; Carrier Proteins/chemistry; Crystallography, X-Ray; Cysteine/chemistry; Disulfides; Dose-Response Relationship, Drug; Guanidine/metabolism; Helicobacter pylori/chemistry; Hexosyltransferases; Hydrolysis; Kinetics; Models, Molecular; Molecular Sequence Data; Muramoylpentapeptide Carboxypeptidase/chemistry; Open Reading Frames; Penicillin-Binding Proteins; Peptidyl Transferases; Protein Binding; Protein Folding; Repetitive Sequences, Amino Acid; Sequence Homology, Amino Acid; Water/chemistry; beta-Lactamases/chemistry

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HELPY:HCPB

GO:0008800: beta-lactamase activity

ECO:0000314:

F

Table 1: Purified HcpB hydrolyzes several antibiotics by opening of the beta-lactam ring, which was monitored by absorption variation.

complete
CACAO 6179

HELPY:HCPB

enables

GO:0008800: beta-lactamase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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