1og3
From Proteopedia
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CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE ART2.2 MUTANT E189I IN COMPLEX WITH NAD
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 ... [(full description)]
About this Structure
1OG3 is a [Single protein] structure of sequence from [Rattus norvegicus] with NAD as [ligand]. Active as [NAD(P)(+)--protein-arginine ADP-ribosyltransferase], with EC number [2.4.2.31]. Structure known Active Site: NAD. 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
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