2ga4
From Proteopedia
Stx2 with adenine
Overview
Stx2 is a protein toxin whose catalytic subunit acts as an N-glycosidase to depurinate a specific adenine base from 28S rRNA. In the holotoxin, the catalytic portion, A1, is linked to the rest of the A subunit, A2, and A2 interacts with the pentameric ring formed by the five B subunits. In order to test whether the holotoxin is active as an N-glycosidase, Stx2 was crystallized in the presence of adenosine and adenine. The crystals diffracted to approximately 1.8 angstroms and showed clear electron density for adenine in the active site. Adenosine had been cleaved, proving that Stx2 is an active N-glycosidase. While the holotoxin is active against small substrates, it would be expected that the B subunits would interfere with the binding of the 28S rRNA.
About this Structure
2GA4 is a Protein complex structure of sequences from Enterobacteria phage 933w. Full crystallographic information is available from OCA.
Reference
Binding of adenine to Stx2, the protein toxin from Escherichia coli O157:H7., Fraser ME, Cherney MM, Marcato P, Mulvey GL, Armstrong GD, James MN, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jul 1;62(Pt, 7):627-30. Epub 2006 Jun 26. PMID:16820678 Page seeded by OCA on Sun May 4 04:52:30 2008
