1qs2

<StructureSection load='1qs2' size='340' side='right' caption='[[1qs2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>

<table><tr><td colspan='2'>[[1qs2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QS2 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qs2 OCA], [http://pdbe.org/1qs2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qs2 RCSB], [http://www.ebi.ac.uk/pdbsum/1qs2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qs2 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:10504727</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1qs2" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 14579]]

[[Category: Carozzi, N B]]

[[Category: Craig, J A]]

[[Category: Han, S]]

[[Category: Putnam, C D]]

[[Category: Tainer, J A]]

[[Category: Alpha-beta protein]]

[[Category: Toxin]]