3drh: Difference between revisions
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==Crystal structure of Lactococcal OppA co-crystallized with Leu-enkephalin in an open conformation== | ==Crystal structure of Lactococcal OppA co-crystallized with Leu-enkephalin in an open conformation== | ||
<StructureSection load='3drh' size='340' side='right' caption='[[3drh]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3drh' size='340' side='right'caption='[[3drh]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3drh]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3drh]] 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=3DRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DRH FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3drf|3drf]], [[3drg|3drg]], [[3dri|3dri]], [[3drj|3drj]], [[3drk|3drk]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3drf|3drf]], [[3drg|3drg]], [[3dri|3dri]], [[3drj|3drj]], [[3drk|3drk]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oppA, llmg_0701 ([ | <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> | ||
<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=3drh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3drh OCA], [https://pdbe.org/3drh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3drh RCSB], [https://www.ebi.ac.uk/pdbsum/3drh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3drh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[ | *[[ABC transporter 3D structures|ABC transporter 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Laclm]] | [[Category: Laclm]] | ||
[[Category: Large Structures]] | |||
[[Category: Berntsson, R P.A]] | [[Category: Berntsson, R P.A]] | ||
[[Category: Doeven, M K]] | [[Category: Doeven, M K]] | ||
Revision as of 11:06, 9 February 2022
Crystal structure of Lactococcal OppA co-crystallized with Leu-enkephalin in an open conformationCrystal structure of Lactococcal OppA co-crystallized with Leu-enkephalin in an open conformation
Structural highlights
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 PubMedOligopeptide-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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