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Literature summary for 1.6.5.9 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
Search for more literature for 1.6.5.9

Crystallization (Commentary)

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

Localization

Localization Comment Organism GeneOntology No. Textmining
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
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mitochondrion Ndi1 protein from Saccharomyces cerevisiae is a monotopic membrane protein, directed to the matrix Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
NADH + H+ + ubiquinone
-
 Saccharomyces cerevisiae NAD+ + ubiquinol
-
 ?

Synonyms

Synonyms Comment Organism
NADH dehydrogenase
-
 Saccharomyces cerevisiae
Ndi1
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
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
NADH binding site structure, overview Saccharomyces cerevisiae

General Information

General Information Comment Organism
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