1njr

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spinqualitylabelsall models 1njr, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

Appr-1-pase, an important and ubiquitous cellular processing enzyme, involved in the tRNA splicing pathway, catalyzes the conversion of, ADP-ribose-1monophosphate (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.

About this Structure

1NJR is a Single protein structure of sequence from Saccharomyces cerevisiae with XYL as ligand. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of ADP-ribose-1-monophosphatase (Appr-1-pase), a ubiquitous cellular processing enzyme., Kumaran D, Eswaramoorthy S, Studier FW, Swaminathan S, Protein Sci. 2005 Mar;14(3):719-26. PMID:15722447

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