PDBsum entry 3d5k

Membrane protein

PDB id: 3d5k

Contents

Protein chains

455 a.a. *

Metals

_NA ×9

_CL

Waters ×539

* Residue conservation analysis

PDB id:

3d5k

Name:

Membrane protein

Title:

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

Structure:

Outer membrane protein oprm. Chain: a, b, c. Synonym: oprm. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 287. Strain: pao1. Gene: oprm, oprk, pa0427. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.40Å R-factor: 0.240 R-free: 0.293

Authors:

G.Phan,I.Broutin,A.Ducruix

Key ref:

G.Phan et al. (2010). Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel. Structure, 18, 507-517. PubMed id: 20399187

Date:

16-May-08 Release date: 02-Jun-09

Protein chains

Q51487  (OPRM_PSEAE) -  Outer membrane protein OprM from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 485 a.a.

Struc: 455 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Structure 18:507-517 (2010)

PubMed id: 20399187

Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel.

G.Phan, H.Benabdelhak, M.B.Lascombe, P.Benas, S.Rety, M.Picard, A.Ducruix, C.Etchebest, I.Broutin.

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."