1og3
From Proteopedia
(New page: 200px<br /> <applet load="1og3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1og3, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1OG3 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with NAD as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.31 2.4.2.31]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OG3 OCA]]. | + | 1OG3 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with NAD as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/NAD(P)(+)--protein-arginine_ADP-ribosyltransferase NAD(P)(+)--protein-arginine ADP-ribosyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.31 2.4.2.31]]. Structure known Active Site: NAD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OG3 OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12939142 12939142] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12939142 12939142] | ||
| + | [[Category: NAD(P)(+)--protein-arginine ADP-ribosyltransferase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 23: | Line 24: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:54:28 2007'' |
Revision as of 11:49, 30 October 2007
|
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
Page seeded by OCA on Tue Oct 30 13:54:28 2007
