2OIG

Crystal structure of RS21-C6 core segment and dm5CTP complex

Summary for 2OIG

• Entry DOI: 10.2210/pdb2oig/pdb
• Related: 2OIE
• Descriptor: RS21-C6, 2'-DEOXY-5-METHYLCYTIDINE 5'-(TETRAHYDROGEN TRIPHOSPHATE) (3 entities in total)
• Functional Keywords: helix, protein-nucleoside triphosphate complex, substrate complex, hydrolase
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm, cytosol : Q9QY93
• Total number of polymer chains: 4
• Total formula weight: 51537.51

Authors

Wu, B.,Liu, Y.,Zhao, Q.,Liao, S.,Zhang, J.,Bartlam, M.,Chen, W.,Rao, Z. (deposition date: 2007-01-11, release date: 2007-03-06, Last modification date: 2024-12-25)

Primary citation

Wu, B.,Liu, Y.,Zhao, Q.,Liao, S.,Zhang, J.,Bartlam, M.,Chen, W.,Rao, Z.
Crystal Structure of RS21-C6, Involved in Nucleoside Triphosphate Pyrophosphohydrolysis
J.Mol.Biol., 367:1405-1412, 2007

PubMed Abstract: 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.

PubMed: 17320107
DOI: 10.1016/j.jmb.2007.01.057

Experimental method

X-RAY DIFFRACTION (3.3 Å)