(Q27639577)

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Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism

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Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism (English)

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crystal structure

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Roberta F. Colman

4

object named as

Roberta F Colman

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author name string

Christopher Ceccarelli

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Neil B Grodsky

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Nandana Ariyaratne

3

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Brian J Bahnson

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language of work or name

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publication date

8 November 2002

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Journal of Biological Chemistry

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277

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43454-62

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45

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Isolation and sequence of a cDNA encoding porcine mitochondrial NADP-specific isocitrate dehydrogenase

1 reference

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Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase

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Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes

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Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-A resolution: a pseudo-Michaelis ternary complex

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Structure of isocitrate dehydrogenase with alpha-ketoglutarate at 2.7-A resolution: conformational changes induced by decarboxylation of isocitrate

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Active site water molecules revealed in the 2.1 A resolution structure of a site-directed mutant of isocitrate dehydrogenase

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Structural basis for a change in substrate specificity: crystal structure of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NADP

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Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase

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Phosphorus-31 nuclear magnetic resonance studies of the binding of nucleotides to NADP+-specific isocitrate dehydrogenase.

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Control of mitochondrial redox balance and cellular defense against oxidative damage by mitochondrial NADP+-dependent isocitrate dehydrogenase

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Expression of pig heart mitochondrial NADP-dependent isocitrate dehydrogenase in Escherichia coli.

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Maltose-binding protein from Escherichia coli.

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Preparation of selenomethionyl proteins for phase determination

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Processing of X-ray diffraction data collected in oscillation mode

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Determination of macromolecular structures from anomalous diffraction of synchrotron radiation

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Automated MAD and MIR structure solution

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Protein structure comparison by alignment of distance matrices

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Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels

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The Protein Data Bank

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ALSCRIPT: a tool to format multiple sequence alignments

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Amino acid substitution matrices from an information theoretic perspective

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Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for Escherichia coli isocitrate dehydrogenase kinase/phosphatase

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Access to phosphorylation in isocitrate dehydrogenase may occur by domain shifting

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Multinuclear NMR studies of the divalent metal binding site of NADP-dependent isocitrate dehydrogenase from pig heart

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Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart NADP-dependent isocitrate dehydrogenase

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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The CCP4 suite: programs for protein crystallography

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Affinity labeling of NADP+-specific isocitrate dehydrogenase by a new fluorescent nucleotide analogue, 2-[(4-bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 2',5'-bisphosphate

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Conformations of the coenzymes and the allosteric activator, ADP, bound to NAD(+)-dependent isocitrate dehydrogenase from pig heart

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Model building and refinement practice

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Identification by mutagenesis of arginines in the substrate binding site of the porcine NADP-dependent isocitrate dehydrogenase

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Evaluation by site-directed mutagenesis of aspartic acid residues in the metal site of pig heart NADP-dependent isocitrate dehydrogenase

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Identifiers

10.1074/JBC.M207306200

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