1qs1
From Proteopedia
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| - | [[Image:1qs1.jpg|left|200px]] | + | [[Image:1qs1.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF VEGETATIVE INSECTICIDAL PROTEIN2 (VIP2)''' | + | {{Structure |
| + | |PDB= 1qs1 |SIZE=350|CAPTION= <scene name='initialview01'>1qs1</scene>, resolution 1.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF VEGETATIVE INSECTICIDAL PROTEIN2 (VIP2)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QS1 is a [ | + | 1QS1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. 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:// | + | 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: Bacillus cereus]] | ||
[[Category: NAD(+) ADP-ribosyltransferase]] | [[Category: NAD(+) ADP-ribosyltransferase]] | ||
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[[Category: insecticial protein]] | [[Category: insecticial protein]] | ||
| - | ''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 13:41:58 2008'' |
Revision as of 11:41, 20 March 2008
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| , resolution 1.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1QS1 is a Protein complex structure of sequences from Bacillus cereus. 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
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