1a26

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[[Image:1a26.jpg|left|200px]]<br /><applet load="1a26" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1a26.jpg|left|200px]]
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caption="1a26, resolution 2.25&Aring;" />
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'''THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH CARBA-NAD'''<br />
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{{Structure
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|PDB= 1a26 |SIZE=350|CAPTION= <scene name='initialview01'>1a26</scene>, resolution 2.25&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CNA:CARBA-NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>CNA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30]
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|GENE=
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}}
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'''THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH CARBA-NAD'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1A26 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CNA:'>CNA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A26 OCA].
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1A26 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A26 OCA].
==Reference==
==Reference==
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The mechanism of the elongation and branching reaction of poly(ADP-ribose) polymerase as derived from crystal structures and mutagenesis., Ruf A, Rolli V, de Murcia G, Schulz GE, J Mol Biol. 1998 Apr 24;278(1):57-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9571033 9571033]
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The mechanism of the elongation and branching reaction of poly(ADP-ribose) polymerase as derived from crystal structures and mutagenesis., Ruf A, Rolli V, de Murcia G, Schulz GE, J Mol Biol. 1998 Apr 24;278(1):57-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9571033 9571033]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: NAD(+) ADP-ribosyltransferase]]
[[Category: NAD(+) ADP-ribosyltransferase]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:51:47 2008''

Revision as of 07:51, 20 March 2008


PDB ID 1a26

Drag the structure with the mouse to rotate
, resolution 2.25Å
Ligands:
Activity: NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30
Coordinates: save as pdb, mmCIF, xml



THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH CARBA-NAD


Overview

The binding site for the acceptor substrate poly(ADP-ribose) in the elongation reaction of the ADP-ribosyl transferase poly(ADP-ribose) polymerase (PARP) was detected by cocrystallizing the enzyme with an NAD+ analogue. The site was confirmed by mutagenesis studies. In conjunction with the binding site of the donor NAD+, the bound acceptor reveals the geometry of the elongation reaction. It shows in particular that the strictly conserved glutamate residue of all ADP-ribosylating enzymes (Glu988 of PARP) facilitates the reaction by polarizing both, donor and acceptor. Moreover, the binding properties of the acceptor site suggest a mechanism for the branching reaction, that also explains the dual specificity of this transferase for elongation and branching, which is unique among polymer-forming enzymes.

About this Structure

1A26 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

The mechanism of the elongation and branching reaction of poly(ADP-ribose) polymerase as derived from crystal structures and mutagenesis., Ruf A, Rolli V, de Murcia G, Schulz GE, J Mol Biol. 1998 Apr 24;278(1):57-65. PMID:9571033

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