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| - | [[Image:1xoc.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1xoc| PDB=1xoc | SCENE= }} | | {{STRUCTURE_1xoc| PDB=1xoc | SCENE= }} |
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| - | '''The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide.'''
| + | ===The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide.=== |
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| - | ==Overview==
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| - | Besides their role as a source of amino acids for Bacillus subtilis, exogenous peptides play important roles in the signalling pathways leading to the development of competence and sporulation. B.subtilis has three peptide transport systems all belonging to the ATP-binding cassette family, a dipeptide permease (Dpp) and two oligopeptide permeases (Opp and App) with overlapping specificity. These comprise a membrane-spanning channel through which the peptide passes, a pair of ATPases which couple ATP hydrolysis to peptide translocation and a lipid-modified, membrane-anchored extracellular "binding-protein" that serves as the receptor for the system. Here, we present the crystal structure of a soluble form of the peptide-binding protein AppA, which has been solved to 1.6 A spacing by anomalous scattering and molecular replacement methods. The structure reveals a protein made of two distinct lobes with a topology similar to those of DppA from Escherichia coli and OppA from Salmonella typhimurium. Examination of the interlobe region reveals an enlarged pocket, containing electron density defining a nonapeptide ligand. The main-chain of the peptide is well defined and makes a series of polar contacts with the protein including salt-bridges at both its termini. The side-chain density is ambiguous in places, consistent with the interpretation that a population of peptides is bound, whose average electron density resembles the amino acid sequence N-VDSKNTSSW-C.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15588833}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15588833 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15588833}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Oligopeptide]] | | [[Category: Oligopeptide]] |
| | [[Category: Transport]] | | [[Category: Transport]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:17:37 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:27:14 2008'' |
Revision as of 08:27, 28 July 2008
Template:STRUCTURE 1xoc
The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide.
Template:ABSTRACT PUBMED 15588833
About this Structure
1XOC is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide., Levdikov VM, Blagova EV, Brannigan JA, Wright L, Vagin AA, Wilkinson AJ, J Mol Biol. 2005 Jan 28;345(4):879-92. PMID:15588833
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