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3nfz

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Crystal structure of murine aminoacylase 3 in complex with N-acetyl-L-tyrosine

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@@ Line 3: / Line 3: @@
 <StructureSection load='3nfz' size='340' side='right'caption='[[3nfz]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3nfz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NFZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3nfz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NFZ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3NF:N-ACETYL-L-TYROSINE'>3NF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.147&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3nh4|3nh4]], [[3nh5|3nh5]], [[3nh8|3nh8]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3NF:N-ACETYL-L-TYROSINE'>3NF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACY-3, Acy3, Aspa2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nfz OCA], [https://pdbe.org/3nfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nfz RCSB], [https://www.ebi.ac.uk/pdbsum/3nfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nfz ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ACY3_MOUSE ACY3_MOUSE]] Plays an important role in deacetylating mercapturic acids in kidney proximal tubules. Also acts on N-acetyl-aromatic amino acids.<ref>PMID:14656720</ref> <ref>PMID:17012540</ref>
+[https://www.uniprot.org/uniprot/ACY3_MOUSE ACY3_MOUSE] Plays an important role in deacetylating mercapturic acids in kidney proximal tubules. Also acts on N-acetyl-aromatic amino acids.<ref>PMID:14656720</ref> <ref>PMID:17012540</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Trichloroethylene (TCE) is one of the most widespread environmental contaminants, which is metabolized to N-acetyl-S-1,2-dichlorovinyl-l-cysteine (NA-DCVC) before being excreted in the urine. Alternatively, NA-DCVC can be deacetylated by aminoacylase 3 (AA3), an enzyme that is highly expressed in the kidney, liver, and brain. NA-DCVC deacetylation initiates the transformation into toxic products that ultimately causes acute renal failure. AA3 inhibition is therefore a target of interest to prevent TCE induced nephrotoxicity. Here we report the crystal structure of recombinant mouse AA3 (mAA3) in the presence of its acetate byproduct and two substrates: N(alpha)-acetyl-l-tyrosine and NA-DCVC. These structures, in conjunction with biochemical data, indicated that AA3 mediates substrate specificity through van der Waals interactions providing a dynamic interaction interface, which facilitates a diverse range of substrates.
-Structures of aminoacylase 3 in complex with acetylated substrates.,Hsieh JM, Tsirulnikov K, Sawaya MR, Magilnick N, Abuladze N, Kurtz I, Abramson J, Pushkin A Proc Natl Acad Sci U S A. 2010 Oct 4. PMID:20921362<ref>PMID:20921362</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3nfz" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 29: / Line 19: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Abramson, J]]
+[[Category: Abramson J]]
-[[Category: Abuladze, N]]
+[[Category: Abuladze N]]
-[[Category: Hsieh, J M]]
+[[Category: Hsieh JM]]
-[[Category: Kurtz, I]]
+[[Category: Kurtz I]]
-[[Category: Magilnick, N]]
+[[Category: Magilnick N]]
-[[Category: Pushkin, A]]
+[[Category: Pushkin A]]
-[[Category: Sawaya, M R]]
+[[Category: Sawaya MR]]
-[[Category: Tsirulnikov, K]]
+[[Category: Tsirulnikov K]]
-[[Category: Hydrolase]]
-[[Category: N-acetyl-l-tryosine]]

3nfz

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Crystal structure of murine aminoacylase 3 in complex with N-acetyl-L-tyrosine

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