4zir
From Proteopedia
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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 [ | + | <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><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='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'>[ | + | <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 == | ||
| - | [ | + | [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;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:26052893</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4zir" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: | + | [[Category: Cocco N]] |
| - | + | [[Category: Karpowich NK]] | |
| - | [[Category: | + | [[Category: Song JM]] |
| - | [[Category: | + | [[Category: Wang DN]] |
| - | [[Category: | + | |
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Current revision
Crystal structure of EcfAA' heterodimer bound to AMPPNP
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