1b1h: Difference between revisions
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<StructureSection load='1b1h' size='340' side='right'caption='[[1b1h]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1b1h' size='340' side='right'caption='[[1b1h]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1b1h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B1H OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[1b1h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B1H FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HPE:HOMOPHENYLALANINE'>HPE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HPE:HOMOPHENYLALANINE'>HPE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b1h OCA], [https://pdbe.org/1b1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b1h RCSB], [https://www.ebi.ac.uk/pdbsum/1b1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b1h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/OPPA_SALTY 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[ | *[[ABC transporter 3D structures|ABC transporter 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:56, 24 February 2021
OLIGO-PEPTIDE BINDING PROTEIN/TRIPEPTIDE (LYS HPE LYS) COMPLEXOLIGO-PEPTIDE BINDING PROTEIN/TRIPEPTIDE (LYS HPE LYS) COMPLEX
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 PubMedThe oligopeptide-binding protein OppA provides a useful model system for studying the physical chemistry underlying noncovalent interactions since it binds a variety of readily synthesized ligands. We have studied the binding of eight closely related tripeptides of the type Lysine-X-Lysine, where X is an abnormal amino acid, by isothermal titration calorimetry (ITC) and X-ray crystallography. The tripeptides fall into three series of ligands, which have been designed to examine the effects of small changes to the central side chain. Three ligands have a primary amine as the second side chain, two have a straight alkane chain, and three have ring systems. The results have revealed a definite preference for the binding of hydrophobic residues over the positively charged side chains, the latter binding only weakly due to unfavorable enthalpic effects. Within the series of positively charged groups, a point of lowest affinity has been identified and this is proposed to arise from unfavorable electrostatic interactions in the pocket, including the disruption of a key salt bridge. Marked entropy-enthalpy compensation is found across the series, and some of the difficulties in designing tightly binding ligands have been highlighted. Relating structure to thermodynamics: the crystal structures and binding affinity of eight OppA-peptide complexes.,Davies TG, Hubbard RE, Tame JR Protein Sci. 1999 Jul;8(7):1432-44. PMID:10422831[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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