Structure NDH-2
ndh-2 structure colored domains
the structure/fold these proteins may divided 3 domains: first dinucleotide binding domain (green in figure), second dinucleotide binding domain (orange in figure) , c-terminal domain (blue in figure).
the first domain responsible noncovalent binding of fad, while second dinucleotide binding domain binds nadh. both these domain structurally organized in rossmann folds, characteristic gxgxxg motif present.
the third domain, c-terminal, responsible protein-membrane interaction. upon expression of c-terminal truncated version of ndh-2, observed intracelular delocalization membrane citoplasm . third domain, part of first domain, partially responsible binding of electron acceptor (quinone).
there crystalographic structures ndh-2 3 different organisms:
staphylococcus aureus (pdb id:4xdb)
caldalkalibacillus thermarum (pdb id:4nwz)
saccharomyces cerevisiae (pdb id:4g73)
^ y. feng, w. li, j. li, j. wang, j. ge, d. xu, y. liu, k. wu, q. zeng, j.-w. wu, c. tian, b. zhou, m. yang, structural insight type-ii mitochondrial nadh dehydrogenases., nature. 491 (2012) 478–82. doi:10.1038/nature11541
^ a.l. rosário, f. v. sena, a.p. batista, t.f. oliveira, d. athayde, m.m. pereira, j. a. brito, m. archer, expression, purification, crystallization , preliminary x-ray diffraction analysis of type ii nadh:quinone oxidoreductase human pathogen staphylococcus aureus, acta crystallogr. sect. f struct. biol. commun. 71 (2015) 477–482. doi:10.1107/s2053230x15005178.
^ y. feng, w. li, j. li, j. wang, j. ge, d. xu, y. liu, k. wu, q. zeng, j.-w. wu, c. tian, b. zhou, m. yang, structural insight type-ii mitochondrial nadh dehydrogenases., nature. 491 (2012) 478–82. doi:10.1038/nature11541
^ a. heikal, y. nakatani, e. dunn, m.r. weimar, c.l. day, e.n. baker, j.s. lott, l.a. sazanov, g.m. cook, structure of bacterial type ii nadh dehydrogenase: monotopic membrane protein essential role in energy generation, mol microbiol. 91 (2014) 950–964. doi:10.1111/mmi.12507.
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