2ILX
Solution structure of catalytic domain of rat 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNP) protein
「1N4T」から置き換えられました2ILX の概要
エントリーDOI | 10.2210/pdb2ilx/pdb |
関連するPDBエントリー | 1N4T 1WOJ 2I3E |
NMR情報 | BMRB: 5202 |
分子名称 | 2',3'-cyclic-nucleotide 3'-phosphodiesterase (1 entity in total) |
機能のキーワード | cnp, cnpase, nervous system, hydrolase |
由来する生物種 | Rattus norvegicus (Norway rat) |
細胞内の位置 | Membrane: P13233 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 24251.83 |
構造登録者 | |
主引用文献 | Kozlov, G.,Denisov, A.Y.,Pomerantseva, E.,Gravel, M.,Braun, P.E.,Gehring, K. Solution structure of the catalytic domain of RICH protein from goldfish. Febs J., 274:1600-1609, 2007 Cited by PubMed Abstract: Regeneration-induced CNPase homolog (RICH) is an axonal growth-associated protein, which is induced in teleost fish upon optical nerve injury. RICH consists of a highly acidic N-terminal domain, a catalytic domain with 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) activity and a C-terminal isoprenylation site. In vitro RICH and mammalian brain CNPase specifically catalyze the hydrolysis of 2',3'-cyclic nucleotides to produce 2'-nucleotides, but the physiologically relevant in vivo substrate remains unknown. Here, we report the NMR structure of the catalytic domain of goldfish RICH and describe its binding to CNPase inhibitors. The structure consists of a twisted nine-stranded antiparallel beta-sheet surrounded by alpha-helices on both sides. Despite significant local differences mostly arising from a seven-residue insert in the RICH sequence, the active site region is highly similar to that of human CNPase. Likewise, refinement of the catalytic domain of rat CNPase using residual dipolar couplings gave improved agreement with the published crystal structure. NMR titrations of RICH with inhibitors point to a similar catalytic mechanism for RICH and CNPase. The results suggest a functional importance for the evolutionarily conserved phosphodiesterase activity and hint of a link with pre-tRNA splicing. PubMed: 17480208DOI: 10.1111/j.1742-4658.2007.05707.x 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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