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3csl
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3csl is ON HOLD until Paper Publication Authors: Krieg, S., Diederichs, K. Description: Structure of the Serratia marcescens hemophore receptor Has...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA and heme== | |
| + | <StructureSection load='3csl' size='340' side='right'caption='[[3csl]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3csl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_marcescens"_(bizio_1823)_trevisan_in_de_toni_and_trevisan_1889 "bacillus marcescens" (bizio 1823) trevisan in de toni and trevisan 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CSL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3csn|3csn]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hasR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=615 "Bacillus marcescens" (Bizio 1823) Trevisan in de Toni and Trevisan 1889]), hasA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=615 "Bacillus marcescens" (Bizio 1823) Trevisan in de Toni and Trevisan 1889])</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=3csl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3csl OCA], [https://pdbe.org/3csl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3csl RCSB], [https://www.ebi.ac.uk/pdbsum/3csl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3csl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/HASA_SERMA HASA_SERMA]] Can bind free heme and also acquire it from hemoglobin. Conveys heme from hemoglobin to the HasR receptor which releases it into the bacterium. HasR alone can take up heme but the synergy between HasA and HasR increases heme uptake 100-fold.<ref>PMID:7937909</ref> <ref>PMID:9171402</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cs/3csl_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3csl ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Gram-negative bacteria use specific heme uptake systems, relying on outer membrane receptors and excreted heme-binding proteins (hemophores) to scavenge and actively transport heme. To unravel the unknown molecular details involved, we present 3 structures of the Serratia marcescens receptor HasR in complex with its hemophore HasA. The transfer of heme over a distance of 9 A from its high-affinity site in HasA into a site of lower affinity in HasR is coupled with the exergonic complex formation of the 2 proteins. Upon docking to the receptor, 1 of the 2 axial heme coordinations of the hemophore is initially broken, but the position and orientation of the heme is preserved. Subsequently, steric displacement of heme by a receptor residue ruptures the other axial coordination, leading to heme transfer into the receptor. | ||
| - | + | Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex.,Krieg S, Huche F, Diederichs K, Izadi-Pruneyre N, Lecroisey A, Wandersman C, Delepelaire P, Welte W Proc Natl Acad Sci U S A. 2009 Jan 27;106(4):1045-50. Epub 2009 Jan 14. PMID:19144921<ref>PMID:19144921</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3csl" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Diederichs, K]] | ||
| + | [[Category: Krieg, S]] | ||
| + | [[Category: Beta-barrel]] | ||
| + | [[Category: Heme]] | ||
| + | [[Category: Hemophore receptor]] | ||
| + | [[Category: Iron]] | ||
| + | [[Category: Membrane protein-heme binding protein complex]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Outer membrane protein]] | ||
| + | [[Category: Secreted]] | ||
| + | [[Category: Tonb box]] | ||
Current revision
Structure of the Serratia marcescens hemophore receptor HasR in complex with its hemophore HasA and heme
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