1idc
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(New page: 200px<br /><applet load="1idc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1idc, resolution 2.5Å" /> '''ISOCITRATE DEHYDROGEN...)
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Revision as of 15:11, 20 November 2007
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ISOCITRATE DEHYDROGENASE FROM E.COLI (MUTANT K230M), STEADY-STATE INTERMEDIATE COMPLEX DETERMINED BY LAUE CRYSTALLOGRAPHY
Overview
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.
About this Structure
1IDC is a Single protein structure of sequence from Escherichia coli with MG and OXS as ligands. Active as Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42 Full crystallographic information is available from OCA.
Reference
Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase., Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE Jr, Stoddard BL, Science. 1995 Jun 2;268(5215):1312-8. PMID:7761851
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