3SYB

Crystal structure of Pseudomonas aeruginosa OccD3 (OpdP)

Summary for 3SYB

• Entry DOI: 10.2210/pdb3syb/pdb
• Related: 3SY7 3SY9 3SYS 3SZD 3SZV 3T0S 3T20 3T24
• Descriptor: Glycine-glutamate dipeptide porin OpdP, SULFATE ION, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (4 entities in total)
• Functional Keywords: beta-barrel, channel, bacterial outer membrane, membrane protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 52568.74

Authors

van den Berg, B.,Eren, E. (deposition date: 2011-07-16, release date: 2012-02-08, Last modification date: 2024-02-28)

Primary citation

Eren, E.,Vijayaraghavan, J.,Liu, J.,Cheneke, B.R.,Touw, D.S.,Lepore, B.W.,Indic, M.,Movileanu, L.,van den Berg, B.
Substrate Specificity within a Family of Outer Membrane Carboxylate Channels.
Plos Biol., 10:e1001242-e1001242, 2012

PubMed Abstract: Many Gram-negative bacteria, including human pathogens such as Pseudomonas aeruginosa, do not have large-channel porins. This results in an outer membrane (OM) that is highly impermeable to small polar molecules, making the bacteria intrinsically resistant towards many antibiotics. In such microorganisms, the majority of small molecules are taken up by members of the OprD outer membrane protein family. Here we show that OprD channels require a carboxyl group in the substrate for efficient transport, and based on this we have renamed the family Occ, for outer membrane carboxylate channels. We further show that Occ channels can be divided into two subfamilies, based on their very different substrate specificities. Our results rationalize how certain bacteria can efficiently take up a variety of substrates under nutrient-poor conditions without compromising membrane permeability. In addition, they explain how channel inactivation in response to antibiotics can cause resistance but does not lead to decreased fitness.

PubMed: 22272184
DOI: 10.1371/journal.pbio.1001242

Experimental method

X-RAY DIFFRACTION (2.7 Å)