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1qs2

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{{STRUCTURE_1qs2| PDB=1qs2 | SCENE= }}
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'''CRYSTAL STRUCTURE OF VIP2 WITH NAD'''
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===CRYSTAL STRUCTURE OF VIP2 WITH NAD===
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==Overview==
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A member of the Bacillus-produced vegetative insecticidal proteins (VIPs) possesses high specificity against the major insect pest, corn rootworms, and belongs to a class of binary toxins and regulators of biological pathways distinct from classical A-B toxins. The 1.5 A resolution crystal structure of the enzymatic ADP-ribosyltransferase component, VIP2, from Bacillus cereus reveals structurally homologous N- and C-terminal alpha/beta domains likely representing the entire class of binary toxins and implying evolutionary relationships between families of ADP-ribosylating toxins. The crystal structure of the kinetically trapped VIP2-NAD complex identifies the NAD binding cleft within the C-terminal enzymatic domain and provides a structural basis for understanding the targeting and catalysis of the medically and environmentally important binary toxins. These structures furthermore provide specific experimental results to help resolve paradoxes regarding the specific mechanism of ADP-ribosylation of actin by implicating ground state destabilization and nicotinamide product sequestration as the major driving forces for catalysis.
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==About this Structure==
==About this Structure==
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[[Category: Binary toxin]]
[[Category: Binary toxin]]
[[Category: Protein-nad complex]]
[[Category: Protein-nad complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:38:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:59:29 2008''

Revision as of 07:59, 28 July 2008

Image:1qs2.png

Template:STRUCTURE 1qs2

CRYSTAL STRUCTURE OF VIP2 WITH NAD

Template:ABSTRACT PUBMED 10504727

About this Structure

Full crystallographic information is available from OCA.

Reference

Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex., Han S, Craig JA, Putnam CD, Carozzi NB, Tainer JA, Nat Struct Biol. 1999 Oct;6(10):932-6. PMID:10504727

Page seeded by OCA on Mon Jul 28 10:59:29 2008

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