1NJR

Crystal structure of yeast ymx7, an ADP-ribose-1''-monophosphatase

1NJR の概要

• エントリーDOI: 10.2210/pdb1njr/pdb
• 分子名称: 32.1 kDa protein in ADH3-RCA1 intergenic region, Xylitol (3 entities in total)
• 機能のキーワード: structural genomics, dimer, two domain organization, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, unknown function
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32727.33

構造登録者

Kumaran, D.,Eswaramoorthy, S.,Studier, F.W.,Swaminathan, S.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2003-01-02, 公開日: 2004-08-17, 最終更新日: 2024-11-13)

主引用文献

Kumaran, D.,Eswaramoorthy, S.,Studier, F.W.,Swaminathan, S.
Structure and mechanism of ADP-ribose-1''-monophosphatase (Appr-1''-pase), a ubiquitous cellular processing enzyme
Protein Sci., 14:719-726, 2005

PubMed Abstract: Appr-1''-pase, an important and ubiquitous cellular processing enzyme involved in the tRNA splicing pathway, catalyzes the conversion of ADP-ribose-1''monophosphate (Appr-1''-p) to ADP-ribose. The structures of the native enzyme from the yeast and its complex with ADP-ribose were determined to 1.9 A and 2.05 A, respectively. Analysis of the three-dimensional structure of this protein, selected as a target in a structural genomics project, reveals its putative function and provides clues to the catalytic mechanism. The structure of the 284-amino acid protein shows a two-domain architecture consisting of a three-layer alphabetaalpha sandwich N-terminal domain connected to a small C-terminal helical domain. The structure of Appr-1''-pase in complex with the product, ADP-ribose, reveals an active-site water molecule poised for nucleophilic attack on the terminal phosphate group. Loop-region residues Asn 80, Asp 90, and His 145 may form a catalytic triad.

PubMed: 15722447
DOI: 10.1110/ps.041132005

実験手法

X-RAY DIFFRACTION (1.9 Å)