 |
PDBsum entry 1gsp
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Endoribonuclease
|
PDB id
|
|
|
|
1gsp
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Hydrolysis of a slow cyclic thiophosphate substrate of rnase t1 analyzed by time-Resolved crystallography.
|
|
|
Authors
|
|
I.Zegers,
R.Loris,
G.Dehollander,
A.Fattah haikal,
F.Poortmans,
J.Steyaert,
L.Wyns.
|
|
|
Ref.
|
|
Nat Struct Biol, 1998,
5,
280-283.
|
|
|
PubMed id
|
|
|
|
|
Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
91%.
|
|
|
|
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.
|
|
|
|
|
|
|
