4bir

From Proteopedia

Revision as of 15:42, 30 October 2007

RIBONUCLEASE T1: FREE HIS92GLN MUTANT

Overview

Histidine-40 is known to participate in phosphodiester transesterification, catalyzed by the enzyme ribonuclease T1. A mutant enzyme with a lysine, replacing the histidine-40 (His40Lys RNase T1) retains considerable, catalytic activity [Steyaert, J., Hallenga, K., Wyns, L., & Stanssens, P., (1990) Biochemistry 29, 9064-9072]. We report on the crystal structures of, His40Lys RNase T1 containing a phosphate anion and a guanosine, 2'-phosphate inhibitor in the active site, respectively. Similar to, previously described structures, the phosphate-containing crystals are of, space group P2(1)2(1)2(1), with one molecule per asymmetric unit (a =, 48.27 A, b = 46.50 A, c = 41.14 A). The complex with 2'-GMP crystallized, in the lower symmetry space group P2(1), with two molecules per ... [(full description)]

About this Structure

4BIR is a [Single protein] structure of sequence from [Aspergillus oryzae] with CA as [ligand]. Active as [Ribonuclease T(1)], with EC number [3.1.27.3]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].

Reference

Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant., Zegers I, Verhelst P, Choe HW, Steyaert J, Heinemann U, Saenger W, Wyns L, Biochemistry. 1992 Nov 24;31(46):11317-25. PMID:1445870

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