4gsp: Difference between revisions

Revision as of 20:13, 21 February 2008

RIBONUCLEASE T1 COMPLEXED WITH 2',3'-CGPS + 3'-GMP, 7 DAYS

OverviewOverview

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.

About this StructureAbout this Structure

4GSP is a Single protein structure of sequence from Aspergillus oryzae with and as ligands. Active as Ribonuclease T(1), with EC number 3.1.27.3 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.

ReferenceReference

Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography., Zegers I, Loris R, Dehollander G, Fattah Haikal A, Poortmans F, Steyaert J, Wyns L, Nat Struct Biol. 1998 Apr;5(4):280-3. PMID:9546218

Page seeded by OCA on Thu Feb 21 19:13:25 2008

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OCA

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:52:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:25 2008''