This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1pb3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1pb3.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1pb3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1pb3| PDB=1pb3 | SCENE= }}
{{STRUCTURE_1pb3| PDB=1pb3 | SCENE= }}
-
'''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
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10902579 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10902579}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Isocitrate dehydrogense,idh]]
[[Category: Isocitrate dehydrogense,idh]]
[[Category: Stereospecificity]]
[[Category: Stereospecificity]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:53:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:29:33 2008''

Revision as of 03:29, 29 July 2008

Template:STRUCTURE 1pb3

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

Template:ABSTRACT PUBMED 10902579

About this Structure

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

Reference

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

Page seeded by OCA on Tue Jul 29 06:29:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools