4GSP
RIBONUCLEASE T1 COMPLEXED WITH 2',3'-CGPS + 3'-GMP, 7 DAYS
Summary for 4GSP
Entry DOI | 10.2210/pdb4gsp/pdb |
Descriptor | RIBONUCLEASE T1, CALCIUM ION, GUANOSINE-3'-MONOPHOSPHATE, ... (5 entities in total) |
Functional Keywords | hydrolase, endoribonuclease |
Biological source | Aspergillus oryzae |
Total number of polymer chains | 1 |
Total formula weight | 11859.26 |
Authors | Zegers, I.,Wyns, L. (deposition date: 1997-12-02, release date: 1998-08-12, Last modification date: 2024-10-30) |
Primary citation | Zegers, I.,Loris, R.,Dehollander, G.,Fattah Haikal, A.,Poortmans, F.,Steyaert, J.,Wyns, L. Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography. Nat.Struct.Biol., 5:280-283, 1998 Cited by PubMed 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. PubMed: 9546218DOI: 10.1038/nsb0498-280 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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