7NYV

Respiratory complex I from Escherichia coli - conformation 3

Summary for 7NYV

• Entry DOI: 10.2210/pdb7nyv/pdb
• Related: 7NYH 7NYR 7NYU 7NZ1
• EMDB information: 12652 12653 12654 12655 12661 13291
• Descriptor: NADH-quinone oxidoreductase subunit B, NADH-quinone oxidoreductase subunit H, NADH-quinone oxidoreductase subunit M, ... (17 entities in total)
• Functional Keywords: nadh:ubiquinone reductase (h+-translocating), oxidative phosphorylation, electron transport
• Biological source: Escherichia coli B; More
• Total number of polymer chains: 13
• Total formula weight: 544313.77

Authors

Kolata, P.,Efremov, R.G. (deposition date: 2021-03-23, release date: 2021-08-25)

Primary citation

Kolata, P.,Efremov, R.G.
Structure of Escherichia coli respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation.
Elife, 10:-, 2021

PubMed Abstract: Respiratory complex I is a multi-subunit membrane protein complex that reversibly couples NADH oxidation and ubiquinone reduction with proton translocation against transmembrane potential. Complex I from is among the best functionally characterized complexes, but its structure remains unknown, hindering further studies to understand the enzyme coupling mechanism. Here, we describe the single particle cryo-electron microscopy (cryo-EM) structure of the entire catalytically active complex I reconstituted into lipid nanodiscs. The structure of this mesophilic bacterial complex I displays highly dynamic connection between the peripheral and membrane domains. The peripheral domain assembly is stabilized by unique terminal extensions and an insertion loop. The membrane domain structure reveals novel dynamic features. Unusual conformation of the conserved interface between the peripheral and membrane domains suggests an uncoupled conformation of the complex. Considering constraints imposed by the structural data, we suggest a new simple hypothetical coupling mechanism for the molecular machine.

PubMed: 34308841
DOI: 10.7554/eLife.68710

Experimental method

ELECTRON MICROSCOPY (3.7 Å)