4hzu
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hzu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Levilactobacillus_brevis Levilactobacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HZU FirstGlance]. <br> | <table><tr><td colspan='2'>[[4hzu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Levilactobacillus_brevis Levilactobacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HZU FirstGlance]. <br> | ||
| - | </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=4hzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hzu OCA], [https://pdbe.org/4hzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hzu RCSB], [https://www.ebi.ac.uk/pdbsum/4hzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hzu ProSAT]</span></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]] 3.53Å</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=4hzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hzu OCA], [https://pdbe.org/4hzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hzu RCSB], [https://www.ebi.ac.uk/pdbsum/4hzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hzu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ECFA2_LEVBA ECFA2_LEVBA] 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] | [https://www.uniprot.org/uniprot/ECFA2_LEVBA ECFA2_LEVBA] 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;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The energy-coupling factor (ECF) transporters constitute a novel family of conserved membrane transporters in prokaryotes that have a similar domain organization to the ATP-binding cassette transporters. Each ECF transporter comprises a pair of cytosolic ATPases (the A and A' components, or EcfA and EcfA'), a membrane-embedded substrate-binding protein (the S component, or EcfS) and a transmembrane energy-coupling component (the T component, or EcfT) that links the EcfA-EcfA' subcomplex to EcfS. The structure and transport mechanism of the quaternary ECF transporter remain largely unknown. Here we report the crystal structure of a nucleotide-free ECF transporter from Lactobacillus brevis at a resolution of 3.5 A. The T component has a horseshoe-shaped open architecture, with five alpha-helices as transmembrane segments and two cytoplasmic alpha-helices as coupling modules connecting to the A and A' components. Strikingly, the S component, thought to be specific for hydroxymethyl pyrimidine, lies horizontally along the lipid membrane and is bound exclusively by the five transmembrane segments and the two cytoplasmic helices of the T component. These structural features suggest a plausible working model for the transport cycle of the ECF transporters. | ||
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| - | Structure of a bacterial energy-coupling factor transporter.,Wang T, Fu G, Pan X, Wu J, Gong X, Wang J, Shi Y Nature. 2013 May 9;497(7448):272-6. doi: 10.1038/nature12045. Epub 2013 Apr 14. PMID:23584587<ref>PMID:23584587</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4hzu" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Structure of a bacterial energy-coupling factor transporter
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