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.


1og4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1og4.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1og4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1og4| PDB=1og4 | SCENE= }}
{{STRUCTURE_1og4| PDB=1og4 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE ART2.2 MUTANT E189A IN COMPLEX WITH NADH'''
+
===CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE ART2.2 MUTANT E189A IN COMPLEX WITH NADH===
-
==Overview==
+
<!--
-
The structures of beta-methylenethiazole-4-carboxamide adenine dinucleotide (TAD), NAD(+), and NADH as bound to ecto-ADP-ribosyltransferase 2.2 from rat and to its mutants E189I and E189A, respectively, have been established. The positions and conformations of NAD(+) and its analogues agree in general with those in other ADP-ribosyltransferases. The kinetic constants for NAD(+) hydrolysis were determined by RP-HPLC. The specific activity amounts to 26 units/mg, which is 6000-fold higher than a previously reported rate and 500-fold higher than the hydrolysis rates of other ADP-ribosyltransferases, confirming that hydrolysis is the major function of this enzyme. On the basis of structures and mutant activities, a catalytic mechanism is proposed. The known auto-ADP-ribosylation of the enzyme at the suggested position R184 is supported by one of the crystal structures where the nucleophile position is occupied by an Neta atom of this arginine which in turn is backed up by the base E159.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12939142}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12939142 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12939142}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Immuno-regulation]]
[[Category: Immuno-regulation]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:48:14 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:38:42 2008''

Revision as of 16:38, 27 July 2008

Image:1og4.png

Template:STRUCTURE 1og4

CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE ART2.2 MUTANT E189A IN COMPLEX WITH NADH

Template:ABSTRACT PUBMED 12939142

About this Structure

1OG4 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat., Ritter H, Koch-Nolte F, Marquez VE, Schulz GE, Biochemistry. 2003 Sep 2;42(34):10155-62. PMID:12939142

Page seeded by OCA on Sun Jul 27 19:38:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1og4"
Personal tools