3nh4

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of murine aminoacylase 3

Structural highlights

3nh4 is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACY3_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 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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pushkin A, Carpenito G, Abuladze N, Newman D, Tsuprun V, Ryazantsev S, Motemoturu S, Sassani P, Solovieva N, Dukkipati R, Kurtz I. Structural characterization, tissue distribution, and functional expression of murine aminoacylase III. Am J Physiol Cell Physiol. 2004 Apr;286(4):C848-56. Epub 2003 Dec 3. PMID:14656720 doi:http://dx.doi.org/10.1152/ajpcell.00192.2003
↑ Newman D, Abuladze N, Scholz K, Dekant W, Tsuprun V, Ryazantsev S, Bondar G, Sassani P, Kurtz I, Pushkin A. Specificity of aminoacylase III-mediated deacetylation of mercapturic acids. Drug Metab Dispos. 2007 Jan;35(1):43-50. Epub 2006 Sep 29. PMID:17012540 doi:http://dx.doi.org/10.1124/dmd.106.012062
↑ Hsieh JM, Tsirulnikov K, Sawaya MR, Magilnick N, Abuladze N, Kurtz I, Abramson J, Pushkin A. Structures of aminoacylase 3 in complex with acetylated substrates. Proc Natl Acad Sci U S A. 2010 Oct 4. PMID:20921362 doi:10.1073/pnas.1006687107

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3nh4"

@@ Line 3: / Line 3: @@
 <StructureSection load='3nh4' size='340' side='right'caption='[[3nh4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3nh4]] 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=3NH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NH4 FirstGlance]. <br>
+<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" 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>
+</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&#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;'>[[3nfz|3nfz]], [[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=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='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=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>
 </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 ==
@@ Line 29: / Line 28: @@
 </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: Mercapturate]]

3nh4

From Proteopedia

Current revision

Crystal structure of murine aminoacylase 3

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox