Structural insight into OprD substrate specificity

Shyamasri Biswas, Mohammad M. Mohammad, Dimki R. Patel, Liviu Movileanu, Bert Van Den Berg

Research output: Contribution to journalArticle

70 Scopus citations


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 β-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.

Original languageEnglish (US)
Pages (from-to)1108-1109
Number of pages2
JournalNature Structural and Molecular Biology
Issue number11
StatePublished - Nov 1 2007

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Biswas, S., Mohammad, M. M., Patel, D. R., Movileanu, L., & Van Den Berg, B. (2007). Structural insight into OprD substrate specificity. Nature Structural and Molecular Biology, 14(11), 1108-1109.