This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1a26
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1a26.jpg|left|200px]] | + | [[Image:1a26.jpg|left|200px]] |
| - | + | ||
| - | '''THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH CARBA-NAD''' | + | {{Structure |
| + | |PDB= 1a26 |SIZE=350|CAPTION= <scene name='initialview01'>1a26</scene>, resolution 2.25Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CNA:CARBA-NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>CNA</scene> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH CARBA-NAD''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1A26 is a [ | + | 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== | ||
| - | 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:// | + | 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]] | ||
| Line 21: | Line 30: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''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
| |||||||
| , 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
Page seeded by OCA on Thu Mar 20 09:51:47 2008
