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5x40

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==CbiO-E166Q==
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==Structure of a CbiO dimer bound with AMPPCP==
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<StructureSection load='5x40' size='340' side='right' caption='[[5x40]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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<StructureSection load='5x40' size='340' side='right'caption='[[5x40]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5x40]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X40 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X40 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5x40]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X40 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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.45&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x3x|5x3x]], [[5x41|5x41]]</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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5x40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x40 OCA], [http://pdbe.org/5x40 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x40 RCSB], [http://www.ebi.ac.uk/pdbsum/5x40 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x40 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=5x40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x40 OCA], [https://pdbe.org/5x40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x40 RCSB], [https://www.ebi.ac.uk/pdbsum/5x40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x40 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CBIO_RHOCB CBIO_RHOCB] Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli; can also transport nickel with a very low affinity. Presumably responsible for energy coupling to the transport system.<ref>PMID:16352848</ref> <ref>PMID:20868747</ref>
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Energy-coupling factor (ECF) transporters are a large family of ATP-binding cassette transporters recently identified in microorganisms. Responsible for micronutrient uptake from the environment, ECF transporters are modular transporters composed of a membrane substrate-binding component EcfS and an ECF module consisting of an integral membrane scaffold component EcfT and two cytoplasmic ATP binding/hydrolysis components EcfA/A'. ECF transporters are classified into groups I and II. Currently, the molecular understanding of group-I ECF transporters is very limited, partly due to a lack of transporter complex structural information. Here, we present structures and structure-based analyses of the group-I cobalt ECF transporter CbiMNQO, whose constituting subunits CbiM/CbiN, CbiQ, and CbiO correspond to the EcfS, EcfT, and EcfA components of group-II ECF transporters, respectively. Through reconstitution of different CbiMNQO subunits and determination of related ATPase and transporter activities, the substrate-binding subunit CbiM was found to stimulate CbiQO's basal ATPase activity. The structure of CbiMQO complex was determined in its inward-open conformation and that of CbiO in beta, gamma-methyleneadenosine 5'-triphosphate-bound closed conformation. Structure-based analyses revealed interactions between different components, substrate-gating function of the L1 loop of CbiM, and conformational changes of CbiO induced by ATP binding and product release within the CbiMNQO transporter complex. These findings enabled us to propose a working model of the CbiMNQO transporter, in which the transport process requires the rotation or toppling of both CbiQ and CbiM, and CbiN might function in coupling conformational changes between CbiQ and CbiM.Cell Research advance online publication 21 March 2017; doi:10.1038/cr.2017.38.
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Structure and mechanism of a group-I cobalt energy coupling factor transporter.,Bao Z, Qi X, Hong S, Xu K, He F, Zhang M, Chen J, Chao D, Zhao W, Li D, Wang J, Zhang P Cell Res. 2017 Mar 21. doi: 10.1038/cr.2017.38. PMID:28322252<ref>PMID:28322252</ref>
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==See Also==
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*[[ABC transporter 3D structures|ABC transporter 3D structures]]
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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 5x40" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bao, Z]]
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[[Category: Large Structures]]
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[[Category: Zhang, P]]
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[[Category: Rhodobacter capsulatus]]
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[[Category: Atpase]]
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[[Category: Bao Z]]
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[[Category: Dimer]]
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[[Category: Qi X]]
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[[Category: Ecf transporter]]
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[[Category: Wang J]]
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[[Category: Transport protein]]
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[[Category: Zhang P]]

Current revision

Structure of a CbiO dimer bound with AMPPCP

PDB ID 5x40

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