1qs1
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(New page: 200px<br /><applet load="1qs1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qs1, resolution 1.5Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 02:15, 25 November 2007
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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. Active as NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30 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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