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Literature summary for 7.6.2.2 extracted from

  • Rai, V.; Gaur, M.; Kumar, A.; Shukla, S.; Komath, S.S.; Prasad, R.
    A novel catalytic mechanism for ATP hydrolysis employed by the N-terminal nucleotide-binding domain of Cdr1p, a multidrug ABC transporter of Candida albicans (2008), Biochim. Biophys. Acta, 1778, 2143-2153.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type an dmutant N-terminal nucleotide binding domains in Escherichia coli strain BL21(DE3) Candida albicans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, both Mg2+ coordination and nucleotide binding contribute to the formation of the active site, entry of Mg2+ into the active site causes the first large conformational change that brings Trp326 and Cys193 in close proximity to each other, besides Trp326, typical Glu238 in the Q-loop also participates in coordination of Mg2+ by the N-terminal nucleotide binding domain Candida albicans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + xenobiotic/in Candida albicans
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ADP + phosphate + xenobiotic/out
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Organism

Organism UniProt Comment Textmining
Candida albicans
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + xenobiotic/in
-
Candida albicans ADP + phosphate + xenobiotic/out
-
?
ATP + H2O + xenobiotic/in the typical Cys193 in Walker A as well as Trp326 and Asp327 in the Walker B of N-terminal nucleotide binding domain of Cdr1p have acquired unique roles in ATP binding and hydrolysis. Asn328 is a gamma-phosphate sensor. ATP docking subsequent to Mg2+ coordination induces further conformational changes, structure analysis, overview Candida albicans ADP + phosphate + xenobiotic/out
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?

Synonyms

Synonyms Comment Organism
Cdr1p
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Candida albicans

Cofactor

Cofactor Comment Organism Structure
ATP
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Candida albicans