Structural Basis of the Substrate Specificity of Bifunctional Isocitrate Dehydrogenase Kinase/Phosphatase
| Autor: | Adam J. Stein, Susan P. Yates, Cassie M. Bryan, Jimin Zheng, Peter J. Myler, Thomas E. Edwards, Wesley C. Van Voorhis, Zongchao Jia, Lance Stewart |
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| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Burkholderia pseudomallei Gram-negative bacteria Protein Conformation Phosphatase medicine.disease_cause Biochemistry Article Substrate Specificity Protein structure Multienzyme Complexes Oxidoreductase Catalytic Domain Gram-Negative Bacteria Escherichia coli medicine Protein Interaction Domains and Motifs Binding site Protein Structure Quaternary chemistry.chemical_classification biology Escherichia coli Proteins biology.organism_classification Molecular biology Isocitrate Dehydrogenase Kinetics Isocitrate dehydrogenase chemistry Phosphorylation Dimerization |
| Zdroj: | Biochemistry. 50:8103-8106 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi200809p |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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