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| | ==Cobalt transporter ATP-binding subunit== | | ==Cobalt transporter ATP-binding subunit== |
| - | <StructureSection load='4mki' size='340' side='right' caption='[[4mki]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='4mki' size='340' side='right'caption='[[4mki]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <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> |
| - | </td></tr><tr id='ligand'><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></td></tr> | + | </td></tr><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> |
| - | <tr id='gene'><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>
| + | <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> |
| - | <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=4mki FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mki OCA], [http://pdbe.org/4mki PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mki RCSB], [http://www.ebi.ac.uk/pdbsum/4mki PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mki ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ECFA2_THETN ECFA2_THETN]] 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 (By similarity). | + | [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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] | + | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis MB4]] |
| - | [[Category: Chai, C L]] | + | [[Category: Large Structures]] |
| - | [[Category: Heymann, D]] | + | [[Category: Chai CL]] |
| - | [[Category: Yu, Y]] | + | [[Category: Heymann D]] |
| - | [[Category: Zhang, L]] | + | [[Category: Yu Y]] |
| - | [[Category: Ecf type cobalt transporter]]
| + | [[Category: Zhang L]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nucleotide-binding domain]]
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| Structural highlights
Function
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]
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chai C, Yu Y, Zhuo W, Zhao H, Li X, Wang N, Chai J, Yang M. Structural basis for a homodimeric ATPase subunit of an ECF transporter. Protein Cell. 2013 Oct;4(10):793-801. doi: 10.1007/s13238-013-3915-y. Epub 2013, Oct 9. PMID:24104393 doi:http://dx.doi.org/10.1007/s13238-013-3915-y
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