6icd: Difference between revisions

Line 1:

[[Image:6icd.~~gif~~|left|200px]]

[[Image:6icd.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE~~'''~~

===REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE===

~~==Overview==~~

<!--

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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_2204109}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 2204109 is the PubMed ID number.

-->

==About this Structure==

Line 27:

Line 31:

[[Category: Sohl, J L.]]

[[Category: Stroud, R M.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May~~ ~~4 22~~:41:24 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:21:05 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:6icd.gif|left|200px]]
+{{Seed}}
+[[Image:6icd.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_6icd|  PDB=6icd  |  SCENE=  }}
-'''REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE'''
+===REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_2204109}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 2204109 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_2204109}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Sohl, J L.]]
 [[Category: Stroud, R M.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:41:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 14:21:05 2008''