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1rtu

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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:34:54 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:03:46 2007''

Revision as of 13:59, 30 October 2007


1rtu, resolution 1.8Å

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USTILAGO SPHAEROGENA RIBONUCLEASE U2

Overview

The crystal structure of purine-specific ribonuclease (RNase) U2 from, Ustilago sphaerogena has been solved by the molecular replacement methods, using RNase T1 as a search model. The structure, with 114 amino acid, residues, 141 water molecules, and a sulfate ion, is refined to an R, factor of 0.143 at 1.8 A resolution. As evidenced by the electron, densities, residues 49 and 50 are revised to Glu 49 and Asp 50, respectively, and also Asp 45 is identified as a beta-isomerized form to, L-isoaspartate with a beta-peptide linkage. RNase U2 consists of a, beta-hairpin at residues from 7 to 14, a 4.4-turn alpha-helix from 16 to, 32, a central beta-sheet with five strands, and a protruding beta-turn, from 74 to 77. As for the catalytic site residues, His 41, Glu 62, and Arg, 85 are located as ... [(full description)]

About this Structure

1RTU is a [Single protein] structure of sequence from [Ustilago sphaerogena] with SO4 as [ligand]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].

Reference

Crystal structure of Ustilago sphaerogena ribonuclease U2 at 1.8 A resolution., Noguchi S, Satow Y, Uchida T, Sasaki C, Matsuzaki T, Biochemistry. 1995 Nov 28;34(47):15583-91. PMID:7492561

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