1A26

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

Summary for 1A26

• Entry DOI: 10.2210/pdb1a26/pdb
• Descriptor: POLY (ADP-RIBOSE) POLYMERASE, CARBA-NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: transferase, glycosyltransferase, nad(+) adp-ribosyltransferase
• Biological source: Gallus gallus (chicken)
• Cellular location: Nucleus : P26446
• Total number of polymer chains: 1
• Total formula weight: 41077.81

Authors

Ruf, A.,Schulz, G.E. (deposition date: 1998-01-16, release date: 1998-05-27, Last modification date: 2024-05-22)

Primary citation

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

PubMed Abstract: 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.

PubMed: 9571033
DOI: 10.1006/jmbi.1998.1673

Experimental method

X-RAY DIFFRACTION (2.25 Å)