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5b57

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==Inward-facing conformation of ABC heme importer BhuUV from Burkholderia cenocepacia==
==Inward-facing conformation of ABC heme importer BhuUV from Burkholderia cenocepacia==
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<StructureSection load='5b57' size='340' side='right' caption='[[5b57]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='5b57' size='340' side='right'caption='[[5b57]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5b57]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B57 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B57 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5b57]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_J2315 Burkholderia cenocepacia J2315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B57 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b58|5b58]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5b57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b57 OCA], [http://pdbe.org/5b57 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b57 RCSB], [http://www.ebi.ac.uk/pdbsum/5b57 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b57 ProSAT]</span></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=5b57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b57 OCA], [https://pdbe.org/5b57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b57 RCSB], [https://www.ebi.ac.uk/pdbsum/5b57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b57 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/B4EKB5_BURCJ B4EKB5_BURCJ]] Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.[HAMAP-Rule:MF_01718][SAAS:SAAS00041320]
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[https://www.uniprot.org/uniprot/B4EKB4_BURCJ B4EKB4_BURCJ]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pathogenic bacteria remove iron from the haem of host tissues and use it as a catalytic center of many enzymes. Haem uptake by pathogenic bacteria is facilitated by the membrane-integrated haem importer, which belongs to the type II ATP-binding cassette (ABC) transporter. Here we present crystal structures of Burkholderia cenocepacia haem importer BhuUV complexed with the periplasmic haem-binding protein BhuT and in the absence of BhuT. The transmembrane helices of these structures show an inward-facing conformation, in which the cytoplasmic gate of the haem translocation pathway is completely open. Since this conformation is found in both the haem- and nucleotide-free form, the structure of BhuUV-T provides the post-translocation state and the missing piece in the transport cycle of the type II importer. Structural comparison with the outward-facing conformation reported for the haem importer ortholog HmuUV from Yersenia pestis gives mechanistic insights into conformational transitions and haem secretion during the haem transport cycle.
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Crystal structure of bacterial haem importer complex in the inward-facing conformation.,Naoe Y, Nakamura N, Doi A, Sawabe M, Nakamura H, Shiro Y, Sugimoto H Nat Commun. 2016 Nov 10;7:13411. doi: 10.1038/ncomms13411. PMID:27830695<ref>PMID:27830695</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 5b57" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Doi, A]]
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[[Category: Burkholderia cenocepacia J2315]]
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[[Category: Nakamura, N]]
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[[Category: Large Structures]]
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[[Category: Naoe, Y]]
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[[Category: Doi A]]
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[[Category: Shiro, Y]]
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[[Category: Nakamura N]]
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[[Category: Sugimoto, H]]
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[[Category: Naoe Y]]
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[[Category: Membrane protein]]
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[[Category: Shiro Y]]
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[[Category: Metal transport]]
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[[Category: Sugimoto H]]
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[[Category: Metal-binding]]
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Current revision

Inward-facing conformation of ABC heme importer BhuUV from Burkholderia cenocepacia

PDB ID 5b57

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