| The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands. | |
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MedLine Citation:
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PMID: 8747465 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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BACKGROUND: The periplasmic oligopeptide-binding protein OppA has a remarkably broad substrate specificity, binding peptides of two or five amino-acid residues with high affinity, but little regard to sequence. It is therefore an ideal system for studying how different chemical groups can be accommodated in a protein interior. The ability of the protein to bind peptides of different lengths has been studied by co-crystallising it with different ligands. RESULTS: Crystals of OppA from Salmonella typhimurium complexed with the peptides Lys-Lys-Lys (KKK) and Lys-Lys-Lys-Ala (KKKA) have been grown in the presence of uranyl ions which form important crystal contacts. These structures have been refined to 1.4 A and 2.1 A, respectively. The ligands are completely enclosed, their side chains pointing into large hydrated cavities and making few strong interactions with the protein. CONCLUSIONS: Tight peptide binding by OppA arises from strong hydrogen bonding and electrostatic interactions between the protein and the main chain of the ligand. Different basic side chains on the protein form salt bridges with the C terminus of peptide ligands of different lengths. |
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Authors:
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J R Tame; E J Dodson; G Murshudov; C F Higgins; A J Wilkinson |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Structure (London, England : 1993) Volume: 3 ISSN: 0969-2126 ISO Abbreviation: Structure Publication Date: 1995 Dec |
Date Detail:
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Created Date: 1996-10-24 Completed Date: 1996-10-24 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 101087697 Medline TA: Structure Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 1395-406 Citation Subset: IM |
Affiliation:
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Department of Chemistry, University of York, UK. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Bacterial Proteins / chemistry*, metabolism Carrier Proteins / chemistry*, metabolism Chemistry, Physical Crystallography, X-Ray HLA Antigens / chemistry, metabolism Hydrogen Bonding Ligands Lipoproteins / chemistry*, metabolism Models, Molecular* Molecular Sequence Data Oligopeptides / metabolism* Physicochemical Phenomena Polylysine / metabolism Protein Binding Protein Structure, Tertiary* Salmonella typhimurium / chemistry* Uranium / chemistry |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Carrier Proteins; 0/HLA Antigens; 0/Ligands; 0/Lipoproteins; 0/Oligopeptides; 0/oligopeptide-binding protein, Salmonella typhimurium; 0/oligopeptide-binding protein, bacteria; 25104-18-1/Polylysine; 7440-61-1/Uranium |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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