1njr

<table><tr><td colspan='2'>[[1njr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NJR FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XYL:D-XYLITOL'>XYL</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YMR087W or YM9582.12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1njr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1njr OCA], [http://pdbe.org/1njr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1njr RCSB], [http://www.ebi.ac.uk/pdbsum/1njr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1njr ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1njr TOPSAN]</span></td></tr>

[[http://www.uniprot.org/uniprot/YMX7_YEAST YMX7_YEAST]] Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing. + phosphate.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15722447</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1njr" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Burley, S K]]

[[Category: Eswaramoorthy, S]]

[[Category: Kumaran, D]]

[[Category: Structural genomic]]

[[Category: Studier, F W]]

[[Category: Swaminathan, S]]

[[Category: Unknown function]]