1b2h: Difference between revisions
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==Oligo-Peptide Binding Protein Complexed with Lysyl-Ornithyl-Lysine== | ==Oligo-Peptide Binding Protein Complexed with Lysyl-Ornithyl-Lysine== | ||
<StructureSection load='1b2h' size='340' side='right' caption='[[1b2h]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1b2h' size='340' side='right'caption='[[1b2h]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1b2h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B2H FirstGlance]. <br> | <table><tr><td colspan='2'>[[1b2h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B2H FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b2/1b2h_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b2/1b2h_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1b2h" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1b2h" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Oligopeptide-binding protein|Oligopeptide-binding protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Davies, T G]] | [[Category: Davies, T G]] | ||
[[Category: Tame, J R.H]] | [[Category: Tame, J R.H]] | ||
[[Category: Peptide binding protein]] | [[Category: Peptide binding protein]] | ||
Revision as of 19:48, 28 August 2019
Oligo-Peptide Binding Protein Complexed with Lysyl-Ornithyl-LysineOligo-Peptide Binding Protein Complexed with Lysyl-Ornithyl-Lysine
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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