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PDBsum entry 1idc

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Oxidoreductase (NAD(a)-choh(d)) PDB id
1idc
Contents
Protein chain
414 a.a.
Ligands
OXS
Metals
_MG

References listed in PDB file
Key reference
Title Mutagenesis and laue structures of enzyme intermediates: isocitrate dehydrogenase.
Authors J.M.Bolduc, D.H.Dyer, W.G.Scott, P.Singer, R.M.Sweet, D.E.Koshland, B.L.Stoddard.
Ref. Science, 1995, 268, 1312-1318. [DOI no: 10.1126/science.7761851]
PubMed id 7761851
Abstract
Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution were used to solve the structures of two sequential intermediates formed during the catalytic actions of isocitrate dehydrogenase. Both intermediates are distinct from the enzyme-substrate and enzyme-product complexes. Mutation of key catalytic residues changed the rate determining steps so that protein and substrate intermediates within the overall reaction pathway could be visualized.
Secondary reference #1
Title Catalytic mechanism of NADP(+)-Dependent isocitrate dehydrogenase: implications from the structures of magnesium-Isocitrate and NADP+ complexes.
Authors J.H.Hurley, A.M.Dean, D.E.Koshland, R.M.Stroud.
Ref. Biochemistry, 1991, 30, 8671-8678. [DOI no: 10.1021/bi00099a026]
PubMed id 1888729
Full text Abstract
Secondary reference #2
Title Regulation of isocitrate dehydrogenase by phosphorylation involves no long-Range conformational change in the free enzyme.
Authors J.H.Hurley, A.M.Dean, P.E.Thorsness, D.E.Koshland, R.M.Stroud.
Ref. J Biol Chem, 1990, 265, 3599-3602.
PubMed id 2406256
Abstract
Secondary reference #3
Title Regulation of an enzyme by phosphorylation at the active site.
Authors J.H.Hurley, A.M.Dean, J.L.Sohl, D.E.Koshland, R.M.Stroud.
Ref. Science, 1990, 249, 1012-1016. [DOI no: 10.1126/science.2204109]
PubMed id 2204109
Full text Abstract
Secondary reference #4
Title Structure of a bacterial enzyme regulated by phosphorylation, Isocitrate dehydrogenase.
Authors J.H.Hurley, P.E.Thorsness, V.Ramalingam, N.H.Helmers, D.E.Koshland, R.M.Stroud.
Ref. Proc Natl Acad Sci U S A, 1989, 86, 8635-8639. [DOI no: 10.1073/pnas.86.22.8635]
PubMed id 2682654
Full text Abstract
PROCHECK
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 Headers

 

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