4MT0

Crystal Structure of the Open State of the Neisseria gonorrhoeae MtrE Outer Membrane Channel

4MT0 の概要

• エントリーDOI: 10.2210/pdb4mt0/pdb
• 関連するPDBエントリー: 4MSY 4MSZ 4MT1 4MT3 4MT4
• 分子名称: MtrE protein, SULFATE ION (3 entities in total)
• 機能のキーワード: beta barrel, membrane protein, tranport protein
• 由来する生物種: Neisseria gonorrhoeae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48624.58

構造登録者

Su, C.-C.,Bolla, J.R.,Yu, E.W. (登録日: 2013-09-18, 公開日: 2014-08-06, 最終更新日: 2024-02-28)

主引用文献

Lei, H.T.,Chou, T.H.,Su, C.C.,Bolla, J.R.,Kumar, N.,Radhakrishnan, A.,Long, F.,Delmar, J.A.,Do, S.V.,Rajashankar, K.R.,Shafer, W.M.,Yu, E.W.
Crystal structure of the open state of the Neisseria gonorrhoeae MtrE outer membrane channel.
Plos One, 9:e97475-e97475, 2014

PubMed Abstract: Active efflux of antimicrobial agents is one of the most important strategies used by bacteria to defend against antimicrobial factors present in their environment. Mediating many cases of antibiotic resistance are transmembrane efflux pumps, composed of one or more proteins. The Neisseria gonorrhoeae MtrCDE tripartite multidrug efflux pump, belonging to the hydrophobic and amphiphilic efflux resistance-nodulation-cell division (HAE-RND) family, spans both the inner and outer membranes of N. gonorrhoeae and confers resistance to a variety of antibiotics and toxic compounds. We here describe the crystal structure of N. gonorrhoeae MtrE, the outer membrane component of the MtrCDE tripartite multidrug efflux system. This trimeric MtrE channel forms a vertical tunnel extending down contiguously from the outer membrane surface to the periplasmic end, indicating that our structure of MtrE depicts an open conformational state of this channel.

PubMed: 24901251
DOI: 10.1371/journal.pone.0097475

実験手法

X-RAY DIFFRACTION (3.292 Å)