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1txz
From Proteopedia
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| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | YMR087W, YM9582.12 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of yeast ymx7, an ADP-ribose-1-monophosphatase, complexed with ADP-ribose
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
1TXZ is a Single protein structure of sequence from Saccharomyces cerevisiae. 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
Page seeded by OCA on Thu Mar 20 14:24:48 2008
Categories: Saccharomyces cerevisiae | Single protein | Burley, S K. | Kumaran, D. | NYSGXRC, New York Structural GenomiX Research Consortium. | Swaminathan, S. | APR | EDO | NA | SO4 | Adp-ribose complex | Dimer | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomic | Two domain organization
