3o7q

From Proteopedia

(Difference between revisions)

Revision as of 16:22, 4 August 2016

Crystal structure of a Major Facilitator Superfamily (MFS) transporter, FucP, in the outward conformation

Structural highlights

3o7q is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3o7p
Gene:	fucP, b2801, JW2772 (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3o7q"

@@ Line 1: / Line 1: @@
 ==Crystal structure of a Major Facilitator Superfamily (MFS) transporter, FucP, in the outward conformation==
 <StructureSection load='3o7q' size='340' side='right' caption='[[3o7q]], [[Resolution|resolution]] 3.14&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o7p|3o7p]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o7q RCSB], [http://www.ebi.ac.uk/pdbsum/3o7q PDBsum]</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=3o7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7q OCA], [http://pdbe.org/3o7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o7q RCSB], [http://www.ebi.ac.uk/pdbsum/3o7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7q ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3o7q ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3o7q" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Lactose Permease|Lactose Permease]]
+*[[Symporter|Symporter]]
 == References ==
 <references/>

3o7q

From Proteopedia

Revision as of 16:22, 4 August 2016

Crystal structure of a Major Facilitator Superfamily (MFS) transporter, FucP, in the outward conformation

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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