2OIE
Crystal structure of RS21-C6 core segment RSCUT
2OIE の概要
エントリーDOI | 10.2210/pdb2oie/pdb |
関連するPDBエントリー | 2OIG |
分子名称 | RS21-C6, SULFATE ION (3 entities in total) |
機能のキーワード | helix, hydrolase |
由来する生物種 | Mus musculus (house mouse) |
細胞内の位置 | Cytoplasm, cytosol : Q9QY93 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 51053.44 |
構造登録者 | |
主引用文献 | 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: 17320107DOI: 10.1016/j.jmb.2007.01.057 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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