Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography

I Zegers; R Loris; G Dehollander; A Fattah Haikal; F Poortmans; J Steyaert; L Wyns; Abdelfattah Haikal

doi:10.1038/nsb0498-280

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Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography

Journal article

Peer reviewed

Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography

I Zegers, R Loris, G Dehollander, A Fattah Haikal, F Poortmans, J Steyaert, L Wyns and Abdelfattah Haikal

Nature structural biology, Vol.5(4), pp.280-283

01/04/1998

DOI: https://doi.org/10.1038/nsb0498-280

PMID: 9546218

Abstract

Aspergillus oryzae - enzymology

Binding Sites

Computer Simulation

Crystallography, X-Ray - methods

Cyclic GMP - analogs & derivatives

Cyclic GMP - chemistry

Cyclic GMP - metabolism

Hydrolysis

Models, Molecular

Molecular Conformation

Molecular Sequence Data

Protein Conformation

Ribonuclease T1 - chemistry

Ribonuclease T1 - metabolism

Substrate Specificity

Thionucleotides - chemistry

Thionucleotides - metabolism

Time Factors

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.

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Title: Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography
Creators - without role: I Zegers - Vrije Universiteit Brussel
R Loris - Vrije Universiteit Brussel
G Dehollander - Vlaams Instituut voor Biotechnologie
A Fattah Haikal
F Poortmans - Vrije Universiteit Brussel
J Steyaert - Vlaams Instituut voor Biotechnologie
L Wyns - Vrije Universiteit Brussel
Abdelfattah Haikal - Islamic University of Al Madinah
Publication Details: Nature structural biology, Vol.5(4), pp.280-283
Identifiers: 9916879108331
Academic Unit: Islamic University of Al Madinah
Language: English
Resource Type: Journal article