1S0J
Trypanosoma cruzi trans-sialidase in complex with MuNANA (Michaelis complex)
Summary for 1S0J
| Entry DOI | 10.2210/pdb1s0j/pdb |
| Related | 1S0I 1S0K |
| Descriptor | trans-sialidase, 4-METHYL-2-OXO-2H-CHROMEN-7-YL 5-(ACETYLAMINO)-3,5-DIDEOXY-L-ERYTHRO-NON-2-ULOPYRANOSIDONIC ACID (3 entities in total) |
| Functional Keywords | transglycosidase, michaelis complex, trypanosoma cruzi, hydrolase |
| Biological source | Trypanosoma cruzi |
| Total number of polymer chains | 1 |
| Total formula weight | 71812.67 |
| Authors | Amaya, M.F.,Watts, A.G.,Damager, I.,Wehenkel, A.,Nguyen, T.,Buschiazzo, A.,Paris, G.,Frasch, A.C.,Withers, S.G.,Alzari, P.M. (deposition date: 2003-12-31, release date: 2004-05-18, Last modification date: 2023-08-23) |
| Primary citation | Amaya, M.F.,Watts, A.G.,Damager, I.,Wehenkel, A.,Nguyen, T.,Buschiazzo, A.,Paris, G.,Frasch, A.C.,Withers, S.G.,Alzari, P.M. Structural Insights into the Catalytic Mechanism of Trypanosoma cruzi trans-Sialidase. Structure, 12:775-784, 2004 Cited by PubMed Abstract: Sialidases are a superfamily of sialic-acid-releasing enzymes that are of significant interest due to their implication as virulence factors in the pathogenesis of a number of diseases. However, extensive studies of viral and microbial sialidases have failed to provide a comprehensive picture of their mechanistic properties, in part because the structures of competent enzyme-substrate complexes and reaction intermediates have never been described. Here we report these structures for the Trypanosoma cruzi trans-sialidase (TcTS), showing that catalysis by sialidases occurs via a similar mechanism to that of other retaining glycosidases, but with some intriguing differences that may have evolved in response to the substrate structure. PubMed: 15130470DOI: 10.1016/j.str.2004.02.036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
Download full validation report
