(Q27730398)

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Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificity

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Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificity (English)

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J H Hurley

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1

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A M Dean

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2

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15 November 1994

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published in

Structure

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volume

2

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page(s)

1007-16

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issue

11

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cites work

Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution

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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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Aromatic rings act as hydrogen bond acceptors

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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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Regulation of an enzyme by phosphorylation at the active site

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Structural mechanisms for domain movements in proteins

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Co-enzyme specificity of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8

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Redesign of the coenzyme specificity of a dehydrogenase by protein engineering

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Structural differences between wild-type NADP-dependent glutathione reductase from Escherichia coli and a redesigned NAD-dependent mutant

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Purification, catalytic properties, and thermal stability of threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermus thermophilus strain HB8.

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Determination of protein molecular weight, hydration, and packing from crystal density.

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Crystallographic R factor refinement by molecular dynamics

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Stereochemical quality of protein structure coordinates

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

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Identifiers

DOI

10.1016/S0969-2126(94)00104-9

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PubMed ID

7881901

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(Q27730398)

Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificity

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