1ctu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ctu.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ctu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ctu| PDB=1ctu | SCENE= }}
{{STRUCTURE_1ctu| PDB=1ctu | SCENE= }}
-
'''TRANSITION-STATE SELECTIVITY FOR A SINGLE OH GROUP DURING CATALYSIS BY CYTIDINE DEAMINASE'''
+
===TRANSITION-STATE SELECTIVITY FOR A SINGLE OH GROUP DURING CATALYSIS BY CYTIDINE DEAMINASE===
-
==Overview==
+
<!--
-
Cytidine deaminase binds transition-state analog inhibitors approximately 10(7) times more tightly than corresponding 3,4-dihydro analogs containing a proton in place of the 4-hydroxyl group. X-ray crystal structures of complexes with the two matched inhibitors differ only near a "trapped" water molecule in the complex with the 3,4-dihydro analog, where contacts are substantially less favorable than those with the hydroxyl group of the transition-state analog. The hydrogen bond between the hydroxyl group and the Glu 104 carboxylate shortens in that complex, and may become a "low-barrier" hydrogen bond, since at the same time the bond between zinc and the Cys 132 thiolate ligand lengthens. These differences must therefore account for most of the differential binding affinity related to catalysis. Moreover, the trapped water molecule retains some of the binding energy stabilizing the hydroxyl group in the transition-state analog complex. To this extent, the ratio of binding affinities for the two compounds is smaller than the true contribution of the hydroxyl group, a conclusion with significant bearing on interpreting difference free energies derived from substituent effects arising from chemical modification and/or mutagenesis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7718553}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7718553 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7718553}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Xiang, S.]]
[[Category: Xiang, S.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:06:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:21:42 2008''

Revision as of 18:21, 30 June 2008

Image:1ctu.png

Template:STRUCTURE 1ctu

TRANSITION-STATE SELECTIVITY FOR A SINGLE OH GROUP DURING CATALYSIS BY CYTIDINE DEAMINASE

Template:ABSTRACT PUBMED 7718553

About this Structure

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

Reference

Transition-state selectivity for a single hydroxyl group during catalysis by cytidine deaminase., Xiang S, Short SA, Wolfenden R, Carter CW Jr, Biochemistry. 1995 Apr 11;34(14):4516-23. PMID:7718553

Page seeded by OCA on Mon Jun 30 21:21:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ctu"
Personal tools