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4WZ7

Crystal structure of mitochondrial NADH:ubiquinone oxidoreductase from Yarrowia lipolytica.

This is a non-PDB format compatible entry.
Summary for 4WZ7
Entry DOI10.2210/pdb4wz7/pdb
DescriptorNADH-ubiquinone oxidoreductase chain 1, 39-kDa subunit, NUGM protein, ... (50 entities in total)
Functional Keywordscomplex i, respiratory chain, oxidoreductase, mitochondria
Biological sourceYarrowia lipolytica
More
Cellular locationMitochondrion membrane ; Multi- pass membrane protein : Q9B6D4 Q9B6E9
Total number of polymer chains67
Total formula weight656099.59
Authors
Wirth, C.,Zickermann, V.,Brandt, U.,Hunte, C. (deposition date: 2014-11-18, release date: 2015-03-25, Last modification date: 2024-10-09)
Primary citationZickermann, V.,Wirth, C.,Nasiri, H.,Siegmund, K.,Schwalbe, H.,Hunte, C.,Brandt, U.
Structural biology. Mechanistic insight from the crystal structure of mitochondrial complex I.
Science, 347:44-49, 2015
Cited by
PubMed Abstract: Proton-pumping complex I of the mitochondrial respiratory chain is among the largest and most complicated membrane protein complexes. The enzyme contributes substantially to oxidative energy conversion in eukaryotic cells. Its malfunctions are implicated in many hereditary and degenerative disorders. We report the x-ray structure of mitochondrial complex I at a resolution of 3.6 to 3.9 angstroms, describing in detail the central subunits that execute the bioenergetic function. A continuous axis of basic and acidic residues running centrally through the membrane arm connects the ubiquinone reduction site in the hydrophilic arm to four putative proton-pumping units. The binding position for a substrate analogous inhibitor and blockage of the predicted ubiquinone binding site provide a model for the "deactive" form of the enzyme. The proposed transition into the active form is based on a concerted structural rearrangement at the ubiquinone reduction site, providing support for a two-state stabilization-change mechanism of proton pumping.
PubMed: 25554780
DOI: 10.1126/science.1259859
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.6 Å)
Structure validation

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数据于2025-06-18公开中

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