1klx: Difference between revisions

Revision as of 10:32, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1klx.png

Template:STRUCTURE 1klx

Helicobacter pylori cysteine rich protein B (hcpB)Helicobacter pylori cysteine rich protein B (hcpB)

Template:ABSTRACT PUBMED 11777911

About this StructureAbout this Structure

1KLX is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Helicobacter pylori cysteine rich protein B (hcpB)'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11777911}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11777911 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11777911}}
 ==About this Structure==
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 [[Category: Right handed super helix]]
 [[Category: Structural genomic]]
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