1pv6: Difference between revisions

Revision as of 19:43, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pv6.png

Template:STRUCTURE 1pv6

Crystal structure of lactose permeaseCrystal structure of lactose permease

Template:ABSTRACT PUBMED 12893935

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

Page seeded by OCA on Mon Jul 28 19:43:18 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1pv6.gif|left|200px]]
+{{Seed}}
+[[Image:1pv6.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1pv6|  PDB=1pv6  |  SCENE=  }}
-'''Crystal structure of lactose permease'''
+===Crystal structure of lactose permease===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12893935}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12893935 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12893935}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Symport]]
 [[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:31:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:43:18 2008''