1a26
From Proteopedia
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| , resolution 2.25Å | |||||||
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| 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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