1b05: Difference between revisions
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<StructureSection load='1b05' size='340' side='right' caption='[[1b05]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1b05' size='340' side='right' caption='[[1b05]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1b05]] is a 2 chain structure | <table><tr><td colspan='2'>[[1b05]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B05 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=U1:URANIUM+ATOM'>U1</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=U1:URANIUM+ATOM'>U1</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b05 OCA], [http://pdbe.org/1b05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b05 RCSB], [http://www.ebi.ac.uk/pdbsum/1b05 PDBsum]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b05 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b05 RCSB], [http://www.ebi.ac.uk/pdbsum/1b05 PDBsum]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1b05" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Tame, J R.H]] | [[Category: Tame, J R.H]] | ||
[[Category: Wilkinson, A J]] | [[Category: Wilkinson, A J]] | ||
[[Category: Peptide binding protein]] | [[Category: Peptide binding protein]] | ||
[[Category: Peptide transport]] | [[Category: Peptide transport]] | ||
Revision as of 04:27, 12 September 2015
Structure of oligo-peptide binding protein complexed with LYS-CYS-LYSStructure of oligo-peptide binding protein complexed with LYS-CYS-LYS
Structural highlights
Function[OPPA_SALTY] This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, it binds peptides up to five amino acids long with high affinity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIsothermal titration calorimetry has been used to study the binding of 20 different peptides to the peptide binding protein OppA, and the crystal structures of the ligand complexes have been refined. This periplasmic binding protein, part of the oligopeptide permease system of Gram negative bacteria, has evolved to bind and enclose small peptides of widely varying sequences. The peptides used in this study have the sequence Lys-X-Lys, where X is any of the 20 commonly occurring amino acids. The various side-chains found at position 2 on the ligand fit into a hydrated pocket. The majority of side-chains are restrained to particular conformations within the pocket. Water molecules act as flexible adapters, matching the hydrogen-bonding requirements of the protein and ligand and shielding charges on the buried ligand. This use of water by OppA to broaden the repertoire of its binding site is not unique, but contrasts sharply with other proteins which use water to help bind ligands highly selectively. Predicting the thermodynamics of binding from the structure of the complexes is highly complicated by the influence of water on the system. Crystallographic and calorimetric analysis of peptide binding to OppA protein.,Sleigh SH, Seavers PR, Wilkinson AJ, Ladbury JE, Tame JR J Mol Biol. 1999 Aug 13;291(2):393-415. PMID:10438628[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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