2olb

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(New page: 200px<br /><applet load="2olb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2olb, resolution 1.4&Aring;" /> '''OLIGOPEPTIDE BINDING ...)
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[[Image:2olb.jpg|left|200px]]<br /><applet load="2olb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2olb, resolution 1.4&Aring;" />
 
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'''OLIGOPEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH TRI-LYSINE'''<br />
 
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==Overview==
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==OLIGOPEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH TRI-LYSINE==
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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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<StructureSection load='2olb' size='340' side='right'caption='[[2olb]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2olb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1olb 1olb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OLB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2olb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2olb OCA], [https://pdbe.org/2olb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2olb RCSB], [https://www.ebi.ac.uk/pdbsum/2olb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2olb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ol/2olb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2olb ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands.,Tame JR, Dodson EJ, Murshudov G, Higgins CF, Wilkinson AJ Structure. 1995 Dec 15;3(12):1395-406. PMID:8747465<ref>PMID:8747465</ref>
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2OLB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with IUM and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1OLB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OLB OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands., Tame JR, Dodson EJ, Murshudov G, Higgins CF, Wilkinson AJ, Structure. 1995 Dec 15;3(12):1395-406. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8747465 8747465]
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</div>
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[[Category: Salmonella typhimurium]]
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<div class="pdbe-citations 2olb" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Tame, J.]]
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[[Category: Wilkinson, A.J.]]
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[[Category: ACT]]
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[[Category: IUM]]
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[[Category: periplasmic]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:13:07 2007''
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==See Also==
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*[[ABC transporter 3D structures|ABC transporter 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Salmonella typhimurium]]
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[[Category: Tame, J]]
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[[Category: Wilkinson, A J]]
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[[Category: Periplasmic]]

Current revision

OLIGOPEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH TRI-LYSINE

PDB ID 2olb

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