2OIE

Crystal structure of RS21-C6 core segment RSCUT

Summary for 2OIE

Entry DOI	10.2210/pdb2oie/pdb
Related	2OIG
Descriptor	RS21-C6, SULFATE ION (3 entities in total)
Functional Keywords	helix, hydrolase
Biological source	Mus musculus (house mouse)
Cellular location	Cytoplasm, cytosol : Q9QY93
Total number of polymer chains	4
Total formula weight	51053.44
Authors	Wu, B.,Liu, Y.,Zhao, Q.,Liao, S.,Zhang, J.,Bartlam, M.,Chen, W.,Rao, Z. (deposition date: 2007-01-10, release date: 2007-03-06, Last modification date: 2023-12-27)
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation