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Literature summary extracted from

  • Iwata, M.; Lee, Y.; Yamashita, T.; Yagi, T.; Iwata, S.; Cameron, A.D.; Maher, M.J.
    The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates (2012), Proc. Natl. Acad. Sci. USA, 109, 15247-15252.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.6.5.9 Ndi1 in its substrate-free, NAD+- and ubiquinone-complexed states, X-ray diffraction structure determination and analysis Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.5.9 membrane Ndi1 is a peripheral membrane protein forming an intimate dimer, in which packing of the monomeric units within the dimer creates an amphiphilic membrane-anchor domain structure, membrane-anchor domain, overview Saccharomyces cerevisiae 16020
-
1.6.5.9 mitochondrion Ndi1 protein from Saccharomyces cerevisiae is a monotopic membrane protein, directed to the matrix Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.5.9 NADH + H+ + ubiquinone Saccharomyces cerevisiae
-
 NAD+ + ubiquinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.6.5.9 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.5.9 additional information NAD+ binds in the second Rossmann domain in a predominantly positively charged cleft, with the nicotinamide ring approaching the re-face of the FAD Saccharomyces cerevisiae ?
-
 ?
1.6.5.9 NADH + H+ + ubiquinone
-
 Saccharomyces cerevisiae NAD+ + ubiquinol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.6.5.9 NADH dehydrogenase
-
 Saccharomyces cerevisiae
1.6.5.9 Ndi1
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.5.9 FAD binding site structure, overview. The isoalloxazine ring of the FAD is positioned between the two Rossmann domains, which define two channels along the interdomain plane that lead to the active site Saccharomyces cerevisiae
1.6.5.9 NADH binding site structure, overview Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
1.6.5.9 additional information Ndi1 protein from Saccharomyces cerevisiae is a monotopic membrane protein, directed to the mitochondrial matrix. It is a peripheral membrane protein forming an intimate dimer, in which packing of the monomeric units within the dimer creates an amphiphilic membrane-anchor domain structure. Structures of the Ndi1–NAD+ and Ndi1–UQ2 complexes show overlapping binding sites for the NAD+ and quinone substrates Saccharomyces cerevisiae