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1njr
From Proteopedia
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|GENE= YMR087W or YM9582.12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= YMR087W or YM9582.12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd02900 Macro_Appr_pase]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd02900 Macro_Appr_pase]</span> | ||
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1njr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1njr OCA], [http://www.ebi.ac.uk/pdbsum/1njr PDBsum | + | |RELATEDENTRY= |
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1njr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1njr OCA], [http://www.ebi.ac.uk/pdbsum/1njr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1njr RCSB]</span> | ||
}} | }} | ||
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[[Category: two domain organization]] | [[Category: two domain organization]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:31:19 2008'' |
Revision as of 19:31, 30 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | YMR087W or YM9582.12 (Saccharomyces cerevisiae) | ||||||
| Domains: | Macro_Appr_pase | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 22:31:19 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
