2o4v

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(New page: 200px<br /><applet load="2o4v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o4v, resolution 1.94&Aring;" /> '''An arginine ladder i...)
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Revision as of 10:56, 21 November 2007

Image:2o4v.gif

2o4v, resolution 1.94Å

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An arginine ladder in OprP mediates phosphate specific transfer across the outer membrane

Overview

The outer membrane protein OprP mediates the transport of essential, phosphate anions into the pathogenic bacterium Pseudomonas aeruginosa., Here we report the crystallographic structure of trimeric OprP at 1.9-A, resolution, revealing an unprecedented 9-residue arginine 'ladder' that, spans from the extracellular surface down through a constriction zone, where phosphate is coordinated. Lysine residues coat the inner periplasmic, surface, creating an 'electropositive sink' that pulls the phosphates, through the eyelet and into the cell.

About this Structure

2O4V is a Single protein structure of sequence from Pseudomonas aeruginosa with CA, PO4, CL, C8E and GOL as ligands. Full crystallographic information is available from OCA.

Reference

An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane., Moraes TF, Bains M, Hancock RE, Strynadka NC, Nat Struct Mol Biol. 2007 Jan;14(1):85-7. Epub 2006 Dec 24. PMID:17187075

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