2GA4
Stx2 with adenine
Summary for 2GA4
| Entry DOI | 10.2210/pdb2ga4/pdb |
| Related | 1R4P 1R4Q |
| Descriptor | Shiga-like toxin II subunit A, Shiga-like toxin II subunit B, SODIUM ION, ... (8 entities in total) |
| Functional Keywords | ab5-toxin, toxin |
| Biological source | Enterobacteria phage 933W More |
| Cellular location | Secreted: P09385 P09386 |
| Total number of polymer chains | 6 |
| Total formula weight | 73698.41 |
| Authors | Fraser, M.E. (deposition date: 2006-03-07, release date: 2006-07-11, Last modification date: 2024-10-30) |
| Primary citation | Fraser, M.E.,Cherney, M.M.,Marcato, P.,Mulvey, G.L.,Armstrong, G.D.,James, M.N. Binding of adenine to Stx2, the protein toxin from Escherichia coli O157:H7. Acta Crystallogr.,Sect.F, 62:627-630, 2006 Cited by PubMed Abstract: 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. PubMed: 16820678DOI: 10.1107/S1744309106021968 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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