4hzu: Difference between revisions
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==Structure of a bacterial energy-coupling factor transporter== | |||
<StructureSection load='4hzu' size='340' side='right' caption='[[4hzu]], [[Resolution|resolution]] 3.53Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hzu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactobacillus_brevis Lactobacillus 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HZU FirstGlance]. <br> | |||
==Function== | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ecfA1, cbiO1, LVIS_1661 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1580 Lactobacillus brevis]), ecfA2, cbiO2, LVIS_1662 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1580 Lactobacillus brevis]), ecfT, LVIS_1660 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1580 Lactobacillus brevis]), LVIS_2151 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1580 Lactobacillus brevis])</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=4hzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hzu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hzu RCSB], [http://www.ebi.ac.uk/pdbsum/4hzu PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/ECFA1_LACBA ECFA1_LACBA]] Part 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). [[http://www.uniprot.org/uniprot/ECFT_LACBA ECFT_LACBA]] Transmembrane (T) component of an 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). [[http://www.uniprot.org/uniprot/ECFA2_LACBA ECFA2_LACBA]] Part 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). | [[http://www.uniprot.org/uniprot/ECFA1_LACBA ECFA1_LACBA]] Part 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). [[http://www.uniprot.org/uniprot/ECFT_LACBA ECFT_LACBA]] Transmembrane (T) component of an 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). [[http://www.uniprot.org/uniprot/ECFA2_LACBA ECFA2_LACBA]] Part 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). | ||
<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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lactobacillus brevis]] | [[Category: Lactobacillus brevis]] | ||
[[Category: Fu, G B | [[Category: Fu, G B]] | ||
[[Category: Pan, X J | [[Category: Pan, X J]] | ||
[[Category: Shi, Y G | [[Category: Shi, Y G]] | ||
[[Category: Wang, T L | [[Category: Wang, T L]] | ||
[[Category: Ecf]] | [[Category: Ecf]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 13:00, 25 December 2014
Structure of a bacterial energy-coupling factor transporter
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