1njr
From Proteopedia
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- | [[Image:1njr.gif|left|200px]] | + | [[Image:1njr.gif|left|200px]] |
- | + | ||
- | '''Crystal structure of yeast ymx7, an ADP-ribose-1''-monophosphatase''' | + | {{Structure |
+ | |PDB= 1njr |SIZE=350|CAPTION= <scene name='initialview01'>1njr</scene>, resolution 1.9Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=XYL:D-XYLITOL'>XYL</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= YMR087W or YM9582.12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of yeast ymx7, an ADP-ribose-1''-monophosphatase''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1NJR is a [ | + | 1NJR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15722447 15722447] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
- | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: two domain organization]] | [[Category: two domain organization]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:57:48 2008'' |
Revision as of 10:57, 20 March 2008
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, resolution 1.9Å | |||||||
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Ligands: | |||||||
Gene: | YMR087W or YM9582.12 (Saccharomyces cerevisiae) | ||||||
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 Thu Mar 20 12:57:48 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. | XYL | Dimer | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomic | Two domain organization