1idm
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(New page: 200px<br /><applet load="1idm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1idm, resolution 2.2Å" /> '''3-ISOPROPYLMALATE DEH...)
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Revision as of 15:11, 20 November 2007
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3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA
Overview
A loop-deleted mutant form of 3-isopropylmalate dehydrogenase from Thermus, thermophilus was constructed to investigate the relationship between the, flexibility of the structure and the thermostability of the enzyme. The, structure of the mutant enzyme was determined by X-ray crystallography and, was found to be almost the same as that of the native enzyme with a, reduced temperature factor. Although the mutant protein had lost the, flexible loop, its function and thermostability had remained unchanged., This phenomenon can be explained by an internal reprieve tolerance, mechanism.
About this Structure
1IDM is a Single protein structure of sequence from Thermus thermophilus. Active as 3-isopropylmalate dehydrogenase, with EC number 1.1.1.85 Full crystallographic information is available from OCA.
Reference
Structure of a loop-deleted variant of 3-isopropylmalate dehydrogenase from Thermus thermophilus: an internal reprieve tolerance mechanism., Sakurai M, Ohzeki M, Miyazaki K, Moriyama H, Sato M, Tanaka N, Oshima T, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):124-8. PMID:15299733
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