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| | ==Crystal Structure of a transporter== | | ==Crystal Structure of a transporter== |
| - | <StructureSection load='4huq' size='340' side='right' caption='[[4huq]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='4huq' size='340' side='right'caption='[[4huq]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4huq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lacba Lacba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HUQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HUQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4huq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Levilactobacillus_brevis_ATCC_367 Levilactobacillus brevis ATCC 367]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HUQ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbiO1, ecfA1, LVIS_1661, unknown transporter ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=387344 LACBA]), ecfA2, cbiO2, LVIS_1662 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=387344 LACBA]), LVIS_0823 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=387344 LACBA]), ecfT, LVIS_1660 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=387344 LACBA])</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]] 2.998Å</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=4huq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4huq OCA], [http://pdbe.org/4huq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4huq RCSB], [http://www.ebi.ac.uk/pdbsum/4huq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4huq 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=4huq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4huq OCA], [https://pdbe.org/4huq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4huq RCSB], [https://www.ebi.ac.uk/pdbsum/4huq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4huq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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/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/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). | + | [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;">
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| - | == Publication Abstract from PubMed ==
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| - | ATP-binding cassette (ABC) transporters, composed of importers and exporters, form one of the biggest protein superfamilies that transport a variety of substrates across the membrane, powered by ATP hydrolysis. Most ABC transporters are composed of two transmembrane domains and two cytoplasmic nucleotide-binding domains. Also, importers from prokaryotes usually have extra solute-binding proteins in the periplasm that are responsible for the binding of substrates. Structures of importers have been reported that suggested a two-state model for the transport mechanism. Energy-coupling factor (ECF) transporters belong to a new class of ATP-binding cassette importers. Each ECF transporter comprises an energy-coupling module consisting of a transmembrane T protein (EcfT), two nucleotide-binding proteins (EcfA and EcfA'), and another transmembrane substrate-specific binding S protein (EcfS). Despite the similarities with ABC transporters, ECF transporters have different organizational and functional properties. The lack of solute-binding proteins in ECF transporters differentiates them clearly from the canonical ABC importers. Previously reported structures of the EcfS proteins RibU and ThiT clearly demonstrated the binding site of substrate riboflavin and thiamine, respectively. However, the organization of the four different components and the transport mechanism of ECF transporters remain unknown. Here we present the structure of an intact folate ECF transporter from Lactobacillus brevis at a resolution of 3 A. This structure was captured in an inward-facing, nucleotide-free conformation with no bound substrate. The folate-binding protein FolT is nearly parallel to the membrane and is bound almost entirely by EcfT, which adopts an L shape and connects to EcfA and EcfA' through two coupling helices. Two conserved XRX motifs from the coupling helices of EcfT have a vital role in energy coupling by docking into EcfA-EcfA'. We propose a transport model that involves a substantial conformational change of FolT.
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| - | Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis.,Xu K, Zhang M, Zhao Q, Yu F, Guo H, Wang C, He F, Ding J, Zhang P Nature. 2013 Apr 14. doi: 10.1038/nature12046. PMID:23584589<ref>PMID:23584589</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4huq" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lacba]] | + | [[Category: Large Structures]] |
| - | [[Category: Xu, K]] | + | [[Category: Levilactobacillus brevis ATCC 367]] |
| - | [[Category: Yu, F]] | + | [[Category: Xu K]] |
| - | [[Category: Zhang, M]] | + | [[Category: Yu F]] |
| - | [[Category: Zhang, P]] | + | [[Category: Zhang M]] |
| - | [[Category: Zhao, Q]] | + | [[Category: Zhang P]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Zhao Q]] |
| - | [[Category: Transporter]]
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