2oie

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2oie, resolution 2.2Å

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Crystal structure of RS21-C6 core segment RSCUT

Overview

RS21-C6, which is highly expressed in all vertebrate genomes and green, plants, is proposed to have nucleoside triphosphate pyrophosphohydrolase, activity. Here, we report the crystal structures of the core fragment of, RS21-C6, named RSCUT, and the complex with the substrate 5-methyl dCTP., The refined structure of RSCUT consists mainly of alpha-helices and shows, formation of a tightly associated tetramer. On the basis of the structure, of the RSCUT-m5dCTP complex and the results of pyrophosphatase activity, assays, several key residues involved in the substrate binding of RS21-C6, have been identified. Tetramer formation is shown to be required for, substrate binding.

About this Structure

2OIE is a Single protein structure of sequence from Mus musculus with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

Crystal Structure of RS21-C6, Involved in Nucleoside Triphosphate Pyrophosphohydrolysis., Wu B, Liu Y, Zhao Q, Liao S, Zhang J, Bartlam M, Chen W, Rao Z, J Mol Biol. 2007 Jan 26;. PMID:17320107

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