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1njr
From Proteopedia
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[[Image:1njr.gif|left|200px]] | [[Image:1njr.gif|left|200px]] | ||
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'''Crystal structure of yeast ymx7, an ADP-ribose-1''-monophosphatase''' | '''Crystal structure of yeast ymx7, an ADP-ribose-1''-monophosphatase''' | ||
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[[Category: Studier, F W.]] | [[Category: Studier, F W.]] | ||
[[Category: Swaminathan, S.]] | [[Category: Swaminathan, S.]] | ||
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| - | [[Category: | + | [[Category: New york structural genomix research consortium]] |
| - | [[Category: | + | [[Category: Nysgxrc]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Two domain organization]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:37:06 2008'' | |
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Revision as of 23:37, 2 May 2008
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. 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 Sat May 3 02:37:06 2008
Categories: Saccharomyces cerevisiae | Single protein | Burley, S K. | Eswaramoorthy, S. | Kumaran, D. | NYSGXRC, New York Structural GenomiX Research Consortium. | Studier, F W. | Swaminathan, S. | Dimer | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomic | Two domain organization
