An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-01

AUTHORS

Trevor F Moraes, Manjeet Bains, Robert E W Hancock, Natalie C J Strynadka

ABSTRACT

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. More... »

PAGES

85-87

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb1189

DOI

http://dx.doi.org/10.1038/nsmb1189

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1013474559

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17187075


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