Structural highlights
Function
[PORD_PSEAE] Porin with a specificity for basic amino acids. Also possesses serine protease activity.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural insight into OprD substrate specificity.,Biswas S, Mohammad MM, Patel DR, Movileanu L, van den Berg B Nat Struct Mol Biol. 2007 Nov;14(11):1108-9. Epub 2007 Oct 21. PMID:17952093[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Trias J, Nikaido H. Protein D2 channel of the Pseudomonas aeruginosa outer membrane has a binding site for basic amino acids and peptides. J Biol Chem. 1990 Sep 15;265(26):15680-4. PMID:2118530
- ↑ Yoshihara E, Gotoh N, Nishino T, Nakae T. Protein D2 porin of the Pseudomonas aeruginosa outer membrane bears the protease activity. FEBS Lett. 1996 Sep 30;394(2):179-82. PMID:8843159
- ↑ Biswas S, Mohammad MM, Patel DR, Movileanu L, van den Berg B. Structural insight into OprD substrate specificity. Nat Struct Mol Biol. 2007 Nov;14(11):1108-9. Epub 2007 Oct 21. PMID:17952093 doi:10.1038/nsmb1304
