1a26

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(New page: 200px<br /><applet load="1a26" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a26, resolution 2.25&Aring;" /> '''THE CATALYTIC FRAGME...)
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caption="1a26, resolution 2.25&Aring;" />
caption="1a26, resolution 2.25&Aring;" />
'''THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH CARBA-NAD'''<br />
'''THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH CARBA-NAD'''<br />
==Overview==
==Overview==
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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.
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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==
==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 CNA 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A26 OCA].
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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].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ruf, A.]]
[[Category: Ruf, A.]]
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[[Category: Schulz, G.E.]]
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[[Category: Schulz, G E.]]
[[Category: CNA]]
[[Category: CNA]]
[[Category: glycosyltransferase]]
[[Category: glycosyltransferase]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:33:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:01 2008''

Revision as of 09:40, 21 February 2008


1a26, resolution 2.25Å

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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 with as ligand. Active as NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30 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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