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| | ==Crystal structure of EcfAA' heterodimer bound to AMPPNP== | | ==Crystal structure of EcfAA' heterodimer bound to AMPPNP== |
| - | <StructureSection load='4zir' size='340' side='right' caption='[[4zir]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='4zir' size='340' side='right'caption='[[4zir]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zir]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZIR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZIR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zir]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZIR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hlu|4hlu]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4zir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zir OCA], [http://pdbe.org/4zir PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zir RCSB], [http://www.ebi.ac.uk/pdbsum/4zir PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zir ProSAT]</span></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=4zir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zir OCA], [https://pdbe.org/4zir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zir RCSB], [https://www.ebi.ac.uk/pdbsum/4zir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zir ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ECFA2_THEMA ECFA2_THEMA]] 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 (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake; uptake does not occur in the absence of RibU or the EcfA1A2T complex.<ref>PMID:23359690</ref> [[http://www.uniprot.org/uniprot/ECFA1_THEMA ECFA1_THEMA]] 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 (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake; uptake does not occur in the absence of RibU or the EcfA1A2T complex.[HAMAP-Rule:MF_01710]<ref>PMID:23359690</ref> | + | [https://www.uniprot.org/uniprot/ECFA2_THEMA ECFA2_THEMA] 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 (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake; uptake does not occur in the absence of RibU or the EcfA1A2T complex.<ref>PMID:23359690</ref> |
| | <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: Cocco, N]] | + | [[Category: Large Structures]] |
| - | [[Category: Karpowich, N K]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Song, J M]] | + | [[Category: Cocco N]] |
| - | [[Category: Wang, D N]]
| + | [[Category: Karpowich NK]] |
| - | [[Category: Abc transporter]] | + | [[Category: Song JM]] |
| - | [[Category: Atpase]] | + | [[Category: Wang DN]] |
| - | [[Category: Hydrolase-inhibitor complex]] | + | |
| - | [[Category: Transmembrane transport]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Vitamin uptake]]
| + | |
| Structural highlights
Function
ECFA2_THEMA 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 (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake; uptake does not occur in the absence of RibU or the EcfA1A2T complex.[1]
Publication Abstract from PubMed
ECF transporters are a family of active transporters for vitamins. They are composed of four subunits: a membrane-embedded substrate-binding subunit (EcfS), a transmembrane coupling subunit (EcfT) and two ATP-binding-cassette ATPases (EcfA and EcfA'). We have investigated the mechanism of the ECF transporter for riboflavin from the pathogen Listeria monocytogenes, LmECF-RibU. Using structural and biochemical approaches, we found that ATP binding to the EcfAA' ATPases drives a conformational change that dissociates the S subunit from the EcfAA'T ECF module. Upon release from the ECF module, the RibU S subunit then binds the riboflavin transport substrate. We also find that S subunits for distinct substrates compete for the ATP-bound state of the ECF module. Our results explain how ECF transporters capture the transport substrate and reproduce the in vivo observations on S-subunit competition for which the family was named.
ATP binding drives substrate capture in an ECF transporter by a release-and-catch mechanism.,Karpowich NK, Song JM, Cocco N, Wang DN Nat Struct Mol Biol. 2015 Jun 8. doi: 10.1038/nsmb.3040. PMID:26052893[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Karpowich NK, Wang DN. Assembly and mechanism of a group II ECF transporter. Proc Natl Acad Sci U S A. 2013 Feb 12;110(7):2534-9. doi:, 10.1073/pnas.1217361110. Epub 2013 Jan 28. PMID:23359690 doi:http://dx.doi.org/10.1073/pnas.1217361110
- ↑ Karpowich NK, Song JM, Cocco N, Wang DN. ATP binding drives substrate capture in an ECF transporter by a release-and-catch mechanism. Nat Struct Mol Biol. 2015 Jun 8. doi: 10.1038/nsmb.3040. PMID:26052893 doi:http://dx.doi.org/10.1038/nsmb.3040
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