3nh5: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Crystal structure of E177A-mutant murine aminoacylase 3==
==Crystal structure of E177A-mutant murine aminoacylase 3==
<StructureSection load='3nh5' size='340' side='right' caption='[[3nh5]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
<StructureSection load='3nh5' size='340' side='right'caption='[[3nh5]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3nh5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NH5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NH5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3nh5]] 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=3NH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NH5 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=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]] 2.094&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nfz|3nfz]], [[3nh4|3nh4]], [[3nh8|3nh8]]</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=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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3nh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nh5 OCA], [https://pdbe.org/3nh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nh5 RCSB], [https://www.ebi.ac.uk/pdbsum/3nh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nh5 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nh5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nh5 RCSB], [http://www.ebi.ac.uk/pdbsum/3nh5 PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[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>  
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>


==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, 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]]

Latest revision as of 13:00, 14 February 2024

Crystal structure of E177A-mutant murine aminoacylase 3Crystal structure of E177A-mutant murine aminoacylase 3

Structural highlights

3nh5 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 2.094Å
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]

See Also

References

  1. ↑ 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
  2. ↑ 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

3nh5, resolution 2.09Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=3nh5&oldid=4059677"