1ide: Difference between revisions

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[[Image:1ide.jpg|left|200px]]
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{{STRUCTURE_1ide|  PDB=1ide  |  SCENE=  }}  
{{STRUCTURE_1ide|  PDB=1ide  |  SCENE=  }}  


'''ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)'''
===ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)===




==Overview==
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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.
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{{ABSTRACT_PUBMED_7761851}}


==About this Structure==
==About this Structure==
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[[Category: Stoddard, B L.]]
[[Category: Stoddard, B L.]]
[[Category: Sweet, R M.]]
[[Category: Sweet, R M.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:52:24 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:47:49 2008''

Revision as of 07:47, 1 July 2008

File:1ide.png

Template:STRUCTURE 1ide

ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)

Template:ABSTRACT PUBMED 7761851

About this Structure

1IDE is a Single protein structure of sequence from Escherichia coli. 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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