3D5K

Crystal structure of the OprM channel in a non-symmetrical space group

Summary for 3D5K

• Entry DOI: 10.2210/pdb3d5k/pdb
• Descriptor: Outer membrane protein oprM, SODIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: membrane protein, channel, beta-alpha-barrel, antibiotic resistance, lipoprotein, membrane, outer membrane, palmitate, transmembrane, transport
• Biological source: Pseudomonas aeruginosa
• Cellular location: Cell outer membrane; Lipid-anchor: Q51487
• Total number of polymer chains: 3
• Total formula weight: 155581.29

Authors

Phan, G.,Broutin, I.,Ducruix, A. (deposition date: 2008-05-16, release date: 2009-06-02, Last modification date: 2024-10-30)

Primary citation

Phan, G.,Benabdelhak, H.,Lascombe, M.B.,Benas, P.,Rety, S.,Picard, M.,Ducruix, A.,Etchebest, C.,Broutin, I.
Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel.
Structure, 18:507-517, 2010

PubMed Abstract: Originally described in bacteria, drug transporters are now recognized as major determinants in antibiotics resistance. For Gram-negative bacteria, the reversible assembly consisting of an inner membrane protein responsible for the active transport, a periplasmic protein, and an exit outer membrane channel achieves transport. The opening of the outer membrane protein OprM from Pseudomonas aeruginosa was modeled through normal mode analysis starting from a new X-ray structure solved at 2.4 A resolution in P2(1)2(1)2(1) space group. The three monomers are not linked by internal crystallographic symmetries highlighting the possible functional differences. This structure is closed at both ends, but modeling allowed for an opening that is not reduced to the classically proposed "iris-like mechanism."

PubMed: 20399187
DOI: 10.1016/j.str.2010.01.018

Experimental method

X-RAY DIFFRACTION (2.4 Å)