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Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase.


ABSTRACT: Isocitrate dehydrogenase kinase/phosphatase (AceK) regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase (ICDH). On the basis of the recently determined structure of the AceK-ICDH complex from Escherichia coli, we have classified the structures of homodimeric NADP(+)-ICDHs to rationalize and predict which organisms likely contain substrates for AceK. One example is Burkholderia pseudomallei (Bp). Here we report a crystal structure of Bp-ICDH that exhibits the necessary structural elements required for AceK recognition. Kinetic analyses provided further confirmation that Bp-ICDH is a substrate for AceK. We conclude that the highly stringent AceK binding sites on ICDH are maintained only in Gram-negative bacteria.

SUBMITTER: Yates SP 

PROVIDER: S-EPMC3354702 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature

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Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase.

Yates Susan P SP   Edwards Thomas E TE   Bryan Cassie M CM   Stein Adam J AJ   Van Voorhis Wesley C WC   Myler Peter J PJ   Stewart Lance J LJ   Zheng Jimin J   Jia Zongchao Z  

Biochemistry 20110902 38


Isocitrate dehydrogenase kinase/phosphatase (AceK) regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase (ICDH). On the basis of the recently determined structure of the AceK-ICDH complex from Escherichia coli, we have classified the structures of homodimeric NADP(+)-ICDHs to rationalize and predict which organisms likely contain substrates for AceK. One example is Burkholderia pseudomallei (Bp). Here we report a crystal structure of Bp-ICDH that exhib  ...[more]

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