3o7q

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

spinqualitylabelsall models 3o7q, resolution 3.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: BNG 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lactose Permease Symporter

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