1njr
From Proteopedia
(New page: 200px<br /><applet load="1njr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1njr, resolution 1.9Å" /> '''Crystal structure of ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1njr.gif|left|200px]]<br /><applet load="1njr" size=" | + | [[Image:1njr.gif|left|200px]]<br /><applet load="1njr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1njr, resolution 1.9Å" /> | caption="1njr, resolution 1.9Å" /> | ||
'''Crystal structure of yeast ymx7, an ADP-ribose-1''-monophosphatase'''<br /> | '''Crystal structure of yeast ymx7, an ADP-ribose-1''-monophosphatase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Appr-1''-pase, an important and ubiquitous cellular processing enzyme | + | Appr-1''-pase, an important and ubiquitous cellular processing enzyme involved in the tRNA splicing pathway, catalyzes the conversion of ADP-ribose-1''monophosphate (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== | ==About this Structure== | ||
| - | 1NJR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with XYL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1NJR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=XYL:'>XYL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJR OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
[[Category: Eswaramoorthy, S.]] | [[Category: Eswaramoorthy, S.]] | ||
[[Category: Kumaran, D.]] | [[Category: Kumaran, D.]] | ||
| - | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
| - | [[Category: Studier, F | + | [[Category: Studier, F W.]] |
[[Category: Swaminathan, S.]] | [[Category: Swaminathan, S.]] | ||
[[Category: XYL]] | [[Category: XYL]] | ||
| Line 28: | Line 28: | ||
[[Category: two domain organization]] | [[Category: two domain organization]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:49 2008'' |
Revision as of 12:06, 21 February 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 with 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
Page seeded by OCA on Thu Feb 21 14:06:49 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 genomics | Two domain organization
