1qs1
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1qs1.jpg|left|200px]] | [[Image:1qs1.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1qs1", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1qs1| PDB=1qs1 | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''CRYSTAL STRUCTURE OF VEGETATIVE INSECTICIDAL PROTEIN2 (VIP2)''' | '''CRYSTAL STRUCTURE OF VEGETATIVE INSECTICIDAL PROTEIN2 (VIP2)''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QS1 OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/10504727 10504727] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10504727 10504727] | ||
| - | [[Category: Bacillus cereus]] | ||
| - | [[Category: NAD(+) ADP-ribosyltransferase]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Carozzi, N B.]] | [[Category: Carozzi, N B.]] | ||
[[Category: Craig, J A.]] | [[Category: Craig, J A.]] | ||
| Line 31: | Line 25: | ||
[[Category: Putnam, C D.]] | [[Category: Putnam, C D.]] | ||
[[Category: Tainer, J A.]] | [[Category: Tainer, J A.]] | ||
| - | [[Category: | + | [[Category: Alpha-beta protein]] |
| - | [[Category: | + | [[Category: Binary toxin]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 03:38, 3 May 2008
CRYSTAL STRUCTURE OF VEGETATIVE INSECTICIDAL PROTEIN2 (VIP2)
Overview
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.
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 Sat May 3 06:38:26 2008
