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==Crystal structure of murine aminoacylase 3== | ==Crystal structure of murine aminoacylase 3== | ||
<StructureSection load='3nh4' size='340' side='right' caption='[[3nh4]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3nh4' size='340' side='right'caption='[[3nh4]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3nh4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3nh4]] 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=3NH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NH4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3nh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nh4 OCA], [https://pdbe.org/3nh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nh4 RCSB], [https://www.ebi.ac.uk/pdbsum/3nh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nh4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3nh4" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Aspartoacylase|Aspartoacylase]] | *[[Aminoacylase 3D structures|Aminoacylase 3D structures]] | ||
*[[Aspartoacylase 3D structures|Aspartoacylase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Abramson | [[Category: Abramson J]] | ||
[[Category: Abuladze | [[Category: Abuladze N]] | ||
[[Category: Hsieh | [[Category: Hsieh JM]] | ||
[[Category: Kurtz | [[Category: Kurtz I]] | ||
[[Category: Magilnick | [[Category: Magilnick N]] | ||
[[Category: Pushkin | [[Category: Pushkin A]] | ||
[[Category: Sawaya | [[Category: Sawaya MR]] | ||
[[Category: Tsirulnikov | [[Category: Tsirulnikov K]] | ||
Latest revision as of 12:15, 6 September 2023
Crystal structure of murine aminoacylase 3Crystal structure of murine aminoacylase 3
Structural highlights
FunctionACY3_MOUSE Plays an important role in deacetylating mercapturic acids in kidney proximal tubules. Also acts on N-acetyl-aromatic amino acids.[1] [2] Publication Abstract from PubMedTrichloroethylene (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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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