4WZ7
Crystal structure of mitochondrial NADH:ubiquinone oxidoreductase from Yarrowia lipolytica.
This is a non-PDB format compatible entry.
Summary for 4WZ7
Entry DOI | 10.2210/pdb4wz7/pdb |
Descriptor | NADH-ubiquinone oxidoreductase chain 1, 39-kDa subunit, NUGM protein, ... (50 entities in total) |
Functional Keywords | complex i, respiratory chain, oxidoreductase, mitochondria |
Biological source | Yarrowia lipolytica More |
Cellular location | Mitochondrion membrane ; Multi- pass membrane protein : Q9B6D4 Q9B6E9 |
Total number of polymer chains | 67 |
Total formula weight | 656099.59 |
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 citation | Zickermann, 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: 25554780DOI: 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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