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Title: Structural Insight into OprD Substrate Specifity

Abstract

OprD proteins form a large family of substrate-specific outer-membrane channels in Gram-negative bacteria. We report here the X-ray crystal structure of OprD from Pseudomonas aeruginosa, which reveals a monomeric 18-stranded beta-barrel characterized by a very narrow pore constriction, with a positively charged basic ladder on one side and an electronegative pocket on the other side. The location of highly conserved residues in OprD suggests that the structure represents the general architecture of OprD channels.

Authors:
; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
959849
Report Number(s):
BNL-82835-2009-JA
TRN: US201016%%993
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Nature Structural and Molecular Biology; Journal Volume: 14
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; ARCHITECTURE; BACTERIA; CRYSTAL STRUCTURE; PROTEINS; PSEUDOMONAS; RESIDUES; SUBSTRATES; national synchrotron light source

Citation Formats

Biswas,S., Mohammad, M., Patel, D., Movileanu, L., and van den Berg, B. Structural Insight into OprD Substrate Specifity. United States: N. p., 2007. Web. doi:10.1038/nsmb1304.
Biswas,S., Mohammad, M., Patel, D., Movileanu, L., & van den Berg, B. Structural Insight into OprD Substrate Specifity. United States. doi:10.1038/nsmb1304.
Biswas,S., Mohammad, M., Patel, D., Movileanu, L., and van den Berg, B. Mon . "Structural Insight into OprD Substrate Specifity". United States. doi:10.1038/nsmb1304.
@article{osti_959849,
title = {Structural Insight into OprD Substrate Specifity},
author = {Biswas,S. and Mohammad, M. and Patel, D. and Movileanu, L. and van den Berg, B.},
abstractNote = {OprD proteins form a large family of substrate-specific outer-membrane channels in Gram-negative bacteria. We report here the X-ray crystal structure of OprD from Pseudomonas aeruginosa, which reveals a monomeric 18-stranded beta-barrel characterized by a very narrow pore constriction, with a positively charged basic ladder on one side and an electronegative pocket on the other side. The location of highly conserved residues in OprD suggests that the structure represents the general architecture of OprD channels.},
doi = {10.1038/nsmb1304},
journal = {Nature Structural and Molecular Biology},
number = ,
volume = 14,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}