7GSP
RIBONUCLEASE T1/2',3'-CGPS, NON-PRODUCTIVE
Summary for 7GSP
Entry DOI | 10.2210/pdb7gsp/pdb |
Descriptor | RIBONUCLEASE T1, PHOSPHATE ION, GUANOSINE-2',3'-CYCLOPHOSPHOROTHIOATE, ... (4 entities in total) |
Functional Keywords | hydrolase, endoribonuclease, ribonuclease, endonuclease |
Biological source | Aspergillus oryzae |
Total number of polymer chains | 2 |
Total formula weight | 23101.87 |
Authors | Zegers, I.,Wyns, L. (deposition date: 1997-12-10, release date: 1998-03-18, Last modification date: 2023-08-09) |
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 (2 Å) |
Structure validation
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