Unknown

Dataset Information

0

Structure and mechanism of ADP-ribose-1''-monophosphatase (Appr-1''-pase), a ubiquitous cellular processing enzyme.


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.

SUBMITTER: Kumaran D 

PROVIDER: S-EPMC2279289 | biostudies-literature | 2005 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structure and mechanism of ADP-ribose-1''-monophosphatase (Appr-1''-pase), a ubiquitous cellular processing enzyme.

Kumaran Desigan D   Eswaramoorthy Subramaniam S   Studier F William FW   Swaminathan Subramanyam S  

Protein science : a publication of the Protein Society 20050301 3


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 c  ...[more]

Similar Datasets

| S-EPMC1235854 | biostudies-literature
| S-EPMC3184140 | biostudies-literature
| S-EPMC6089346 | biostudies-literature
| S-EPMC4050725 | biostudies-literature
| S-EPMC4030884 | biostudies-literature
| S-EPMC3812366 | biostudies-literature
| S-EPMC2785691 | biostudies-literature
| S-EPMC2792023 | biostudies-literature
| S-EPMC3278890 | biostudies-literature
| S-EPMC9476175 | biostudies-literature