3drf

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Current revision (08:24, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3drf' size='340' side='right'caption='[[3drf]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='3drf' size='340' side='right'caption='[[3drf]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3drf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Laclm Laclm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DRF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3drf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._cremoris_MG1363 Lactococcus lactis subsp. cremoris MG1363]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DRF FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3drg|3drg]], [[3drh|3drh]], [[3dri|3dri]], [[3drj|3drj]], [[3drk|3drk]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oppA, llmg_0701 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=416870 LACLM])</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=3drf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3drf OCA], [https://pdbe.org/3drf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3drf RCSB], [https://www.ebi.ac.uk/pdbsum/3drf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3drf ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3drf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3drf OCA], [https://pdbe.org/3drf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3drf RCSB], [https://www.ebi.ac.uk/pdbsum/3drf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3drf ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A2RJ53_LACLM A2RJ53_LACLM]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=3drf ConSurf].
</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=3drf ConSurf].
<div style="clear:both"></div>
<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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Oligopeptide-binding protein A (OppA) from Lactococcus lactis binds peptides of an exceptionally wide range of lengths (4-35 residues), with no apparent sequence preference. Here, we present the crystal structures of OppA in the open- and closed-liganded conformations. The structures directly explain the protein's phenomenal promiscuity. A huge cavity allows binding of very long peptides, and a lack of constraints for the position of the N and C termini of the ligand is compatible with binding of peptides with varying lengths. Unexpectedly, the peptide's amino-acid composition (but not the exact sequence) appears to have a function in selection, with a preference for proline-rich peptides containing at least one isoleucine. These properties can be related to the physiology of the organism: L. lactis is auxotrophic for branched chain amino acids and favours proline-rich caseins as a source of amino acids. We propose a new mechanism for peptide selection based on amino-acid composition rather than sequence.
 
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The structural basis for peptide selection by the transport receptor OppA.,Berntsson RP, Doeven MK, Fusetti F, Duurkens RH, Sengupta D, Marrink SJ, Thunnissen AM, Poolman B, Slotboom DJ EMBO J. 2009 Mar 19. PMID:19300437<ref>PMID:19300437</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 3drf" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Laclm]]
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[[Category: Lactococcus lactis subsp. cremoris MG1363]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Berntsson, R P.A]]
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[[Category: Berntsson RP-A]]
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[[Category: Doeven, M K]]
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[[Category: Doeven MK]]
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[[Category: Duurkens, R H]]
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[[Category: Duurkens RH]]
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[[Category: Marrink, S J]]
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[[Category: Marrink S-J]]
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[[Category: Poolman, B]]
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[[Category: Poolman B]]
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[[Category: Sengupta, D]]
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[[Category: Sengupta D]]
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[[Category: Slotboom, D J]]
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[[Category: Slotboom D-J]]
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[[Category: Thunnissen, A M]]
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[[Category: Thunnissen A-M]]
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[[Category: Oligo-peptide binding]]
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[[Category: Peptide binding protein]]
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[[Category: Venus fly-trap]]
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[[Category: Voluminous binding cavity]]
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Current revision

Lactococcal OppA complexed with an endogenous peptide in the closed conformation

PDB ID 3drf

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