1klx
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= HP0336 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori]) | |GENE= HP0336 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1klx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1klx OCA], [http://www.ebi.ac.uk/pdbsum/1klx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1klx RCSB]</span> | ||
}} | }} | ||
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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:50:26 2008'' |
Revision as of 18:50, 30 March 2008
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| , resolution 1.950Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | HP0336 (Helicobacter pylori) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Helicobacter pylori cysteine rich protein B (hcpB)
Overview
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.
About this Structure
1KLX is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.
Reference
The crystal structure of Helicobacter pylori cysteine-rich protein B reveals a novel fold for a penicillin-binding protein., Luthy L, Grutter MG, Mittl PR, J Biol Chem. 2002 Mar 22;277(12):10187-93. Epub 2002 Jan 2. PMID:11777911
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