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1TXZ

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

1TXZ の概要
エントリーDOI10.2210/pdb1txz/pdb
関連するPDBエントリー1NJR
分子名称Hypothetical 32.1 kDa protein in ADH3-RCA1 intergenic region, SULFATE ION, SODIUM ION, ... (6 entities in total)
機能のキーワードstructural genomics, dimer, two domain organization, adp-ribose complex, 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32942.75
構造登録者
Kumaran, D.,Swaminathan, S.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2004-07-06, 公開日: 2004-11-30, 最終更新日: 2023-08-23)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.05 Å)
構造検証レポート
Validation report summary of 1txz
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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