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| | ==Crystal structure of the E.coli Fucose:proton symporter, FucP (N162A)== | | ==Crystal structure of the E.coli Fucose:proton symporter, FucP (N162A)== |
| - | <StructureSection load='3o7p' size='340' side='right' caption='[[3o7p]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='3o7p' size='340' side='right'caption='[[3o7p]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3o7p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O7P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3o7p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O7P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</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]] 3.196Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o7q|3o7q]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fucP, b2801, JW2772 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3o7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7p OCA], [https://pdbe.org/3o7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o7p RCSB], [https://www.ebi.ac.uk/pdbsum/3o7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7p ProSAT]</span></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=3o7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7p OCA], [http://pdbe.org/3o7p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o7p RCSB], [http://www.ebi.ac.uk/pdbsum/3o7p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7p ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FUCP_ECOLI FUCP_ECOLI]] Mediates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell (symport system). Can also transport L-galactose and D-arabinose, but at reduced rates compared with L-fucose. Is not able to transport L-rhamnose and L-arabinose.<ref>PMID:2829831</ref> | + | [https://www.uniprot.org/uniprot/FUCP_ECOLI FUCP_ECOLI] Mediates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell (symport system). Can also transport L-galactose and D-arabinose, but at reduced rates compared with L-fucose. Is not able to transport L-rhamnose and L-arabinose.<ref>PMID:2829831</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| | *[[Lactose Permease|Lactose Permease]] | | *[[Lactose Permease|Lactose Permease]] |
| - | *[[Symporter|Symporter]] | + | *[[Symporter 3D structures|Symporter 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Dang, S Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Sun, L F]] | + | [[Category: Dang SY]] |
| - | [[Category: Wang, J]] | + | [[Category: Sun LF]] |
| - | [[Category: Yan, N]] | + | [[Category: Wang J]] |
| - | [[Category: L-fucose]] | + | [[Category: Yan N]] |
| - | [[Category: Multi-pass membrane protein]]
| + | |
| - | [[Category: Symporter]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Transporter]]
| + | |
| Structural highlights
Function
FUCP_ECOLI Mediates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell (symport system). Can also transport L-galactose and D-arabinose, but at reduced rates compared with L-fucose. Is not able to transport L-rhamnose and L-arabinose.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The major facilitator superfamily (MFS) transporters are an ancient and widespread family of secondary active transporters. In Escherichia coli, the uptake of l-fucose, a source of carbon for microorganisms, is mediated by an MFS proton symporter, FucP. Despite intensive study of the MFS transporters, atomic structure information is only available on three proteins and the outward-open conformation has yet to be captured. Here we report the crystal structure of FucP at 3.1 A resolution, which shows that it contains an outward-open, amphipathic cavity. The similarly folded amino and carboxyl domains of FucP have contrasting surface features along the transport path, with negative electrostatic potential on the N domain and hydrophobic surface on the C domain. FucP only contains two acidic residues along the transport path, Asp 46 and Glu 135, which can undergo cycles of protonation and deprotonation. Their essential role in active transport is supported by both in vivo and in vitro experiments. Structure-based biochemical analyses provide insights into energy coupling, substrate recognition and the transport mechanism of FucP.
Structure of a fucose transporter in an outward-open conformation.,Dang S, Sun L, Huang Y, Lu F, Liu Y, Gong H, Wang J, Yan N Nature. 2010 Oct 7;467(7316):734-8. Epub 2010 Sep 26. PMID:20877283[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bradley SA, Tinsley CR, Muiry JA, Henderson PJ. Proton-linked L-fucose transport in Escherichia coli. Biochem J. 1987 Dec 1;248(2):495-500. PMID:2829831
- ↑ Dang S, Sun L, Huang Y, Lu F, Liu Y, Gong H, Wang J, Yan N. Structure of a fucose transporter in an outward-open conformation. Nature. 2010 Oct 7;467(7316):734-8. Epub 2010 Sep 26. PMID:20877283 doi:10.1038/nature09406
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