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1njr

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|PDB= 1njr |SIZE=350|CAPTION= <scene name='initialview01'>1njr</scene>, resolution 1.9&Aring;
|PDB= 1njr |SIZE=350|CAPTION= <scene name='initialview01'>1njr</scene>, resolution 1.9&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=XYL:D-XYLITOL'>XYL</scene>
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=XYL:D-XYLITOL'>XYL</scene>
|ACTIVITY=
|ACTIVITY=
|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>
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|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.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1njr RCSB]</span>
}}
}}
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[[Category: Studier, F W.]]
[[Category: Studier, F W.]]
[[Category: Swaminathan, S.]]
[[Category: Swaminathan, S.]]
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[[Category: XYL]]
 
[[Category: dimer]]
[[Category: dimer]]
[[Category: new york structural genomix research consortium]]
[[Category: new york structural genomix research consortium]]
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[[Category: two domain organization]]
[[Category: two domain organization]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:57:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:58:36 2008''

Revision as of 03:58, 26 March 2008


PDB ID 1njr

Drag the structure with the mouse to rotate
, resolution 1.9Å
Ligands: ,
Gene: YMR087W or YM9582.12 (Saccharomyces cerevisiae)
Domains: Macro_Appr_pase
Resources: FirstGlance, OCA, PDBsum, JenaLib, 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

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