5icd

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[[Image:5icd.gif|left|200px]]
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{{STRUCTURE_5icd| PDB=5icd | SCENE= }}
{{STRUCTURE_5icd| PDB=5icd | SCENE= }}
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'''REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE'''
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===REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE===
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==Overview==
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The isocitrate dehydrogenase of Escherichia coli is an example of a ubiquitous class of enzymes that are regulated by covalent modification. In the three-dimensional structure of the enzyme-substrate complex, isocitrate forms a hydrogen bond with Ser113, the site of regulatory phosphorylation. The structures of Asp113 and Glu113 mutants, which mimic the inactivation of the enzyme by phosphorylation, show minimal conformational changes from wild type, as in the phosphorylated enzyme. Calculations based on observed structures suggest that the change in electrostatic potential when a negative charge is introduced either by phosporylation or site-directed mutagenesis is sufficient to inactivate the enzyme. Thus, direct interaction at a ligand binding site is an alternative mechanism to induced conformational changes from an allosteric site in the regulation of protein activity by phosphorylation.
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The line below this paragraph, {{ABSTRACT_PUBMED_2204109}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 2204109 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2204109}}
==About this Structure==
==About this Structure==
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[[Category: Sohl, J L.]]
[[Category: Sohl, J L.]]
[[Category: Stroud, R M.]]
[[Category: Stroud, R M.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:35:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:04:58 2008''

Revision as of 11:04, 3 July 2008

Template:STRUCTURE 5icd

REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE

Template:ABSTRACT PUBMED 2204109

About this Structure

5ICD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Regulation of an enzyme by phosphorylation at the active site., Hurley JH, Dean AM, Sohl JL, Koshland DE Jr, Stroud RM, Science. 1990 Aug 31;249(4972):1012-6. PMID:2204109

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