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.


1hlw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hlw.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1hlw.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hlw| PDB=1hlw | SCENE= }}
{{STRUCTURE_1hlw| PDB=1hlw | SCENE= }}
-
'''STRUCTURE OF THE H122A MUTANT OF THE NUCLEOSIDE DIPHOSPHATE KINASE'''
+
===STRUCTURE OF THE H122A MUTANT OF THE NUCLEOSIDE DIPHOSPHATE KINASE===
-
==Overview==
+
<!--
-
We have explored the ability of a nucleoside diphosphate kinase (NDPK) mutant in which the nucleophilic histidine has been replaced by glycine (H122G) to transfer phosphate from ATP to alcohols of varying pK(a), size, shape, and polarity. This cavity mutant does indeed act as a primitive alcohol kinase. The rate of its phosphoryl transfer to alcohols varies considerably, with values spanning a DeltaDeltaG(double dagger) range of 4 kcal/mol, whereas the alcohols have very similar intrinsic reactivities. Analysis of these results suggests that the ability to carry out phosphoryl transfer within the cavity is not a simple function of being small enough to enter the cavity, but rather is a complex function of steric, solvation, entropic, van der Waals packing, and electrostatic properties of the alcohol. In addition, large differences are observed between the reactivities of alcohols within the nucleophile cavity of H122G and the reactivities of the same alcohols within the nucleophile cavity of H122A, a mutant NDPK that differs from H122G by a single methyl group within the cavity. The crystal structures of the two cavity mutants are very similar to one another and to wild-type NDPK, providing no evidence for a structurally perturbed active site. The differences in reactivity between the two mutant proteins illustrate a fundamental limitation of energetic analysis from site-directed mutagenesis: although removal of a side chain is generally considered to be a conservative change, the energetic effects of any given mutation are inextricably linked to the molecular properties of the created cavity and the surrounding protein environment.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11148034}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11148034 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11148034}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Kinase]]
[[Category: Kinase]]
[[Category: Phosphotransferase]]
[[Category: Phosphotransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:59:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:22:31 2008''

Revision as of 05:22, 1 July 2008

Image:1hlw.png

Template:STRUCTURE 1hlw

STRUCTURE OF THE H122A MUTANT OF THE NUCLEOSIDE DIPHOSPHATE KINASE

Template:ABSTRACT PUBMED 11148034

About this Structure

1HLW is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.

Reference

Chemical rescue of phosphoryl transfer in a cavity mutant: a cautionary tale for site-directed mutagenesis., Admiraal SJ, Meyer P, Schneider B, Deville-Bonne D, Janin J, Herschlag D, Biochemistry. 2001 Jan 16;40(2):403-13. PMID:11148034

Page seeded by OCA on Tue Jul 1 08:22:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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