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1klx
From Proteopedia
(New page: 200px<br /><applet load="1klx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1klx, resolution 1.950Å" /> '''Helicobacter pylori...) |
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| - | [[Image:1klx.gif|left|200px]]<br /><applet load="1klx" size=" | + | [[Image:1klx.gif|left|200px]]<br /><applet load="1klx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1klx, resolution 1.950Å" /> | caption="1klx, resolution 1.950Å" /> | ||
'''Helicobacter pylori cysteine rich protein B (hcpB)'''<br /> | '''Helicobacter pylori cysteine rich protein B (hcpB)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Colonization of the gastric mucosa with the spiral-shaped Gram-negative | + | 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== | ==About this Structure== | ||
| - | 1KLX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http:// | + | 1KLX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KLX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gruetter, M | + | [[Category: Gruetter, M G.]] |
[[Category: Luethy, L.]] | [[Category: Luethy, L.]] | ||
| - | [[Category: Mittl, P | + | [[Category: Mittl, P R.E.]] |
[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
[[Category: modular structure']] | [[Category: modular structure']] | ||
| Line 21: | Line 21: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:32 2008'' |
Revision as of 11:35, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 13:35:32 2008
