3dms

Publication Abstract from PubMed

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.

Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase.,Yates SP, Edwards TE, Bryan CM, Stein AJ, Van Voorhis WC, Myler PJ, Stewart LJ, Zheng J, Jia Z Biochemistry. 2011 Sep 27;50(38):8103-6. Epub 2011 Sep 2. PMID:21870819^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.