1pb3: Difference between revisions

Revision as of 06:29, 29 July 2008

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File:1pb3.png

Template:STRUCTURE 1pb3

Sites of binding and orientation in a four location model for protein stereospecificity.Sites of binding and orientation in a four location model for protein stereospecificity.

Template:ABSTRACT PUBMED 10902579

About this StructureAbout this Structure

1PB3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Sites of binding and orientation in a four-location model for protein stereospecificity., Mesecar AD, Koshland DE Jr, IUBMB Life. 2000 May;49(5):457-66. PMID:10902579

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Sites of binding and orientation in a four location model for protein stereospecificity.'''
+===Sites of binding and orientation in a four location model for protein stereospecificity.===
-==Overview==
+<!--
-The stereospecificity of the enzyme isocitrate dehydrogenase was examined by steady-state kinetics and x-ray crystallography. The enzyme has the intriguing property that the apoenzyme in the absence of divalent metal showed a selectivity for the inactive l-enantiomer of the substrate isocitrate, whereas the enzyme containing magnesium showed selectivity for the physiologically active d-enantiomer. The hydrogen atom on the C2 carbon that is transferred during the reaction was, in both the d- and l-isocitrate complexes, in an orientation very close to that expected for delivery of a hydride ion to the cosubstrate NADP+. The beta-carboxylate that is eliminated as a CO2 molecule during the reaction occupied the same site on the protein in both the d- and l-isocitrate complexes. In addition, the C3 carbon was in the same protein site in both the d- and l-enantiomers. Only the fourth group, the OH atom, was in a very different position in the apo enzyme and in the metal-containing complexes. A four-location model is necessary to explain the enantiomeric specificity of IDH in contrast to the conventional three-point attachment model. The thermodynamic and kinetic ramifications of this model are explored.
+The line below this paragraph, {{ABSTRACT_PUBMED_10902579}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10902579}}
 ==About this Structure==
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 [[Category: Isocitrate dehydrogense,idh]]
 [[Category: Stereospecificity]]
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