4mki

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==Cobalt transporter ATP-binding subunit==
==Cobalt transporter ATP-binding subunit==
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<StructureSection load='4mki' size='340' side='right' caption='[[4mki]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='4mki' size='340' side='right'caption='[[4mki]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4mki]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MKI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MKI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4mki]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis_MB4 Caldanaerobacter subterraneus subsp. tengcongensis MB4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MKI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MKI FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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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]] 2.3&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ecfA2, cbiO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273068 Caldanaerobacter subterraneus subsp. tengcongensis])</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=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mki FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mki OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mki RCSB], [http://www.ebi.ac.uk/pdbsum/4mki PDBsum]</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=4mki FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mki OCA], [https://pdbe.org/4mki PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mki RCSB], [https://www.ebi.ac.uk/pdbsum/4mki PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mki ProSAT]</span></td></tr>
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<table>
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</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/ECFA2_CALS4 ECFA2_CALS4] ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.[HAMAP-Rule:MF_01710]
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The transition metal cobalt, an essential cofactor for many enzymes in prokaryotes, is taken up by several specific transport systems. The CbiMNQO protein complex belongs to type-1 energy-coupling factor (ECF) transporters and is a widespread group of microbial cobalt transporters. CbiO is the ATPase subunit (A-component) of the cobalt transporting system in the gram-negative thermophilic bacterium Thermoanaerobacter tengcongensis. Here we report the crystal structure of a nucleotide-free CbiO at a resolution of 2.3 A. CbiO contains an N-terminal canonical nucleotide-binding domain (NBD) and C-terminal helical domain. Structural and biochemical data show that CbiO forms a homodimer mediated by the NBD and the C-terminal domain. Interactions mainly via conserved hydrophobic amino acids between the two C-terminal domains result in formation of a four-helix bundle. Structural comparison with other ECF transporters suggests that non-conserved residues outside the T-component binding groove in the A component likely act as a specificity determinant for T components. Together, our data provide information on understanding of the structural organization and interaction of the CbiMNQO system.
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Structural basis for a homodimeric ATPase subunit of an ECF transporter.,Chai C, Yu Y, Zhuo W, Zhao H, Li X, Wang N, Chai J, Yang M Protein Cell. 2013 Oct;4(10):793-801. doi: 10.1007/s13238-013-3915-y. Epub 2013, Oct 9. PMID:24104393<ref>PMID:24104393</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]]
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[[Category: Caldanaerobacter subterraneus subsp. tengcongensis MB4]]
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[[Category: Chai, C L.]]
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[[Category: Large Structures]]
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[[Category: Heymann, D.]]
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[[Category: Chai CL]]
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[[Category: Yu, Y.]]
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[[Category: Heymann D]]
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[[Category: Zhang, L.]]
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[[Category: Yu Y]]
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[[Category: Ecf type cobalt transporter]]
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[[Category: Zhang L]]
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[[Category: Hydrolase]]
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[[Category: Nucleotide-binding domain]]
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Current revision

Cobalt transporter ATP-binding subunit

PDB ID 4mki

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