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.


1tad

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1tad.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1tad.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1tad| PDB=1tad | SCENE= }}
{{STRUCTURE_1tad| PDB=1tad | SCENE= }}
-
'''GTPASE MECHANISM OF GPROTEINS FROM THE 1.7-ANGSTROM CRYSTAL STRUCTURE OF TRANSDUCIN ALPHA-GDP-ALF4-'''
+
===GTPASE MECHANISM OF GPROTEINS FROM THE 1.7-ANGSTROM CRYSTAL STRUCTURE OF TRANSDUCIN ALPHA-GDP-ALF4-===
-
==Overview==
+
<!--
-
Aluminium fluoride (AIF-4) activates members of the heterotrimeric G-protein (G alpha beta gamma) family by binding to inactive G alpha.GDP near the site occupied by the gamma-phosphate in G alpha.GTP (ref. 3). Here we describe the crystal structure of transducin alpha.GDP activated with aluminium fluoride (Gt alpha.GDP.AIF-4.H2O) at 1.7 A, a resolution sufficient to establish the coordination geometry of the bound aluminium fluoride as well as the extensive network of direct and water-mediated interactions that stabilize it. These observations are derived from three independent representations in the asymmetric unit, eliminating any chance of drawing conclusions based on stereochemistry imposed by crystal packing. Surprisingly, aluminium fluoride activates G alpha.GDP by binding with a geometry resembling a pentavalent intermediate for GTP hydrolysis. The stabilizing interactions involve not only residues that interact with the gamma-phosphate in Gt alpha.GTP gamma S, but also conserved residues for GTPase activity. Thus the Gt alpha.GDP.AIF-4.H2O structure provides new insight into the mechanism of GTP hydrolysis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7969474}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7969474 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7969474}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Sondek, J.]]
[[Category: Sondek, J.]]
[[Category: Gtp-binding protein]]
[[Category: Gtp-binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:44:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:16:24 2008''

Revision as of 05:16, 29 July 2008

Image:1tad.png

Template:STRUCTURE 1tad

GTPASE MECHANISM OF GPROTEINS FROM THE 1.7-ANGSTROM CRYSTAL STRUCTURE OF TRANSDUCIN ALPHA-GDP-ALF4-

Template:ABSTRACT PUBMED 7969474

About this Structure

1TAD is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4., Sondek J, Lambright DG, Noel JP, Hamm HE, Sigler PB, Nature. 1994 Nov 17;372(6503):276-9. PMID:7969474

Page seeded by OCA on Tue Jul 29 08:16:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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