PDBsum entry 3d5k

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protein metals Protein-protein interface(s) links
Membrane protein PDB id
Protein chains
455 a.a. *
_NA ×9
Waters ×539
* Residue conservation analysis
PDB id:
Name: Membrane protein
Title: Crystal structure of the oprm channel in a non-symmetrical s
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.
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
16-May-08     Release date:   02-Jun-09    
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Protein chains
Pfam   ArchSchema ?
Q51487  (OPRM_PSEAE) -  Outer membrane protein OprM
485 a.a.
455 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   3 terms 
  Biological process     transport   3 terms 
  Biochemical function     transporter activity     3 terms  


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.
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."