2oie
From Proteopedia
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. 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 Apr 13;367(5):1405-12. Epub 2007 Jan 26. PMID:17320107 Page seeded by OCA on Sun May 4 10:59:06 2008
Categories: Mus musculus | Single protein | Bartlam, M. | Chen, W. | Liao, S. | Liu, Y. | Rao, Z. | Wu, B. | Zhang, J. | Zhao, Q. | Helix
