1a26: Difference between revisions

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[[Image:1a26.~~jpg~~|left|200px]]

[[Image:1a26.png|left|200px]]

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

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

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9571033}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9571033 is the PubMed ID number.

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==About this Structure==

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[[Category: Glycosyltransferase]]

[[Category: Transferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 09~~:41:50 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:49:58 2008''

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-[[Image:1a26.jpg|left|200px]]
+{{Seed}}
+[[Image:1a26.png|left|200px]]
 <!--
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 {{STRUCTURE_1a26|  PDB=1a26  |  SCENE=  }}
-'''THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH CARBA-NAD'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9571033}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9571033 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9571033}}
 ==About this Structure==
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 [[Category: Glycosyltransferase]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:41:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:49:58 2008''