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| {{STRUCTURE_1qs1| PDB=1qs1 | SCENE= }} | | {{STRUCTURE_1qs1| PDB=1qs1 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF VEGETATIVE INSECTICIDAL PROTEIN2 (VIP2)'''
| | ===CRYSTAL STRUCTURE OF VEGETATIVE INSECTICIDAL PROTEIN2 (VIP2)=== |
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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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10504727}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10504727 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10504727}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Binary toxin]] | | [[Category: Binary toxin]] |
| [[Category: Insecticial protein]] | | [[Category: Insecticial protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:38:26 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:21:12 2008'' |
