1pv6: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1pv7|1PV7]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pv6 OCA], [http://www.ebi.ac.uk/pdbsum/1pv6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pv6 RCSB]</span>
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[[Category: transport]]
[[Category: transport]]


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Revision as of 23:05, 30 March 2008

File:1pv6.gif


PDB ID 1pv6

Drag the structure with the mouse to rotate
, resolution 3.5Å
Related: 1PV7


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of lactose permease


OverviewOverview

Membrane transport proteins that transduce free energy stored in electrochemical ion gradients into a concentration gradient are a major class of membrane proteins. We report the crystal structure at 3.5 angstroms of the Escherichia coli lactose permease, an intensively studied member of the major facilitator superfamily of transporters. The molecule is composed of N- and C-terminal domains, each with six transmembrane helices, symmetrically positioned within the permease. A large internal hydrophilic cavity open to the cytoplasmic side represents the inward-facing conformation of the transporter. The structure with a bound lactose homolog, beta-D-galactopyranosyl-1-thio-beta-D-galactopyranoside, reveals the sugar-binding site in the cavity, and residues that play major roles in substrate recognition and proton translocation are identified. We propose a possible mechanism for lactose/proton symport (co-transport) consistent with both the structure and a large body of experimental data.

About this StructureAbout this Structure

1PV6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structure and mechanism of the lactose permease of Escherichia coli., Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, Iwata S, Science. 2003 Aug 1;301(5633):610-5. PMID:12893935

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