Title | Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography. |
Publication Type | Journal Article |
Year of Publication | 1998 |
Authors | Zegers, I., R. Loris, G. Dehollander, F. A Haikal, F. Poortmans, J. Steyaert, and L. Wyns |
Journal | Nat Struct Biol |
Volume | 5 |
Issue | 4 |
Pagination | 280-3 |
Date Published | 1998 Apr |
ISSN | 1072-8368 |
Keywords | Aspergillus oryzae, Binding Sites, Computer Simulation, Crystallography, X-Ray, Cyclic GMP, Hydrolysis, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Protein Conformation, Ribonuclease T1, Substrate Specificity, Thionucleotides, Time Factors |
Abstract | Here we present a time-resolved crystallographic analysis of the hydrolysis of exo (Sp) guanosine 2',3'-cyclophosphorothioate by RNase T1. The use of a slow substrate and fast crystallization methods made it possible to perform the study with conventional data-collection techniques. The results support the idea that the hydrolysis reaction proceeds through a mechanism that is the inverse of the transesterification reaction. In addition, the structures provide an explanation for the differential behavior of RNase T1 towards exo- and endo-cyclic thiophosphates. |
Alternate Journal | Nat. Struct. Biol. |
PubMed ID | 9546218 |
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