5AZO

Crystal structure of a membrane protein from Pseudomonas aeruginosa

Summary for 5AZO

• Entry DOI: 10.2210/pdb5azo/pdb
• Related: 5AZP 5AZS
• Descriptor: Multidrug efflux outer membrane protein OprN (1 entity in total)
• Functional Keywords: alpha barrel, beta barrel, membrane protein
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
• Total number of polymer chains: 1
• Total formula weight: 49686.19

Authors

Yonehara, R.,Yamashita, E.,Nakagawa, A. (deposition date: 2015-10-21, release date: 2016-06-08, Last modification date: 2023-11-08)

Primary citation

Yonehara, R.,Yamashita, E.,Nakagawa, A.
Crystal structures of OprN and OprJ, outer membrane factors of multidrug tripartite efflux pumps of Pseudomonas aeruginosa.
Proteins, 84:759-769, 2016

PubMed Abstract: The genome of Pseudomonas aeruginosa encodes tripartite efflux pumps that extrude functionally and structurally dissimilar antibiotics from the bacterial cell. MexAB-OprM, MexCD-OprJ, MexEF-OprN, and MexXY-OprM are the main tripartite efflux pumps responsible for multidrug resistance in P. aeruginosa. The outer membrane factors OprN, OprJ, and OprM are essential components of functional tripartite efflux pumps. To elucidate the structural basis of multidrug resistance, we determined the crystal structures of OprN and OprJ. These structures revealed several features, including tri-acylation of the N-terminal cysteine, a small pore in the β-barrel domain, and a tightly sealed gate in the α-barrel domain. Despite the overall similarity of OprN, OprJ, and OprM, a comparison of their structures and electrostatic distributions revealed subtle differences at the periplasmic end of the α-barrel domain. These results suggested that the overall structures of these outer membrane factors are specifically optimized for particular tripartite efflux pumps. Proteins 2016; 84:759-769. © 2016 Wiley Periodicals, Inc.

PubMed: 26914226
DOI: 10.1002/prot.25022

Experimental method

X-RAY DIFFRACTION (2.7 Å)