2ODJ

Crystal structure of the outer membrane protein OprD from Pseudomonas aeruginosa

Summary for 2ODJ

• Entry DOI: 10.2210/pdb2odj/pdb
• Descriptor: Porin D, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (2 entities in total)
• Functional Keywords: outer membrane protein, beta-barrel, amino acid transport, membrane protein
• Biological source: Pseudomonas aeruginosa
• Cellular location: Cell outer membrane; Multi-pass membrane protein: P32722
• Total number of polymer chains: 2
• Total formula weight: 97339.25

Authors

Biswas, S.,van den Berg, B. (deposition date: 2006-12-22, release date: 2007-10-16, Last modification date: 2024-10-30)

Primary citation

Biswas, S.,Mohammad, M.M.,Patel, D.R.,Movileanu, L.,van den Berg, B.
Structural insight into OprD substrate specificity.
Nat.Struct.Mol.Biol., 14:1108-1109, 2007

PubMed 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.

PubMed: 17952093
DOI: 10.1038/nsmb1304

Experimental method

X-RAY DIFFRACTION (2.9 Å)