2bir

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Image:2bir.gif

2bir, resolution 2.30Å

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ADDITIVITY OF SUBSTRATE BINDING IN RIBONUCLEASE T1 (Y42A MUTANT)

Overview

It has been established that Tyr-42, Tyr-45, and Glu-46 take part in a, structural motif that renders guanine specificity to ribonuclease T1. We, report on the impact of Tyr-42, Tyr-45, and Glu-46 substitutions on the, guanine specificity of RNase T1. The Y42A and E46A mutations profoundly, affect substrate binding. No such effect is observed for Y45A RNase T1., From the kinetics of the Y42A/Y45A and Y42A/E46A double mutants, we, conclude that these pairs of residues contribute to guanine specificity in, a mutually independent way. From our results, it appears that the, energetic contribution of aromatic face-to-face stacking interactions may, be significant if polycyclic molecules, such as guanine, are involved.

About this Structure

2BIR is a [Single protein] structure of sequence from [Aspergillus oryzae] with CA and 2GP as [ligands]. Full crystallographic information is available from [OCA].

Reference

Additivity of protein-guanine interactions in ribonuclease T1., Loverix S, Doumen J, Steyaert J, J Biol Chem. 1997 Apr 11;272(15):9635-9. PMID:9092491

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