3NH4
Crystal structure of murine aminoacylase 3
Summary for 3NH4
Entry DOI | 10.2210/pdb3nh4/pdb |
Related | 3NFZ 3NH5 3NH8 |
Descriptor | Aspartoacylase-2, ZINC ION, CESIUM ION, ... (7 entities in total) |
Functional Keywords | mercapturates, hydrolase |
Biological source | Mus musculus (mouse) |
Cellular location | Apical cell membrane; Peripheral membrane protein: Q91XE4 |
Total number of polymer chains | 1 |
Total formula weight | 37000.61 |
Authors | Hsieh, J.M.,Tsirulnikov, K.,Sawaya, M.R.,Magilnick, N.,Abuladze, N.,Kurtz, I.,Abramson, J.,Pushkin, A. (deposition date: 2010-06-14, release date: 2010-10-20, Last modification date: 2023-09-06) |
Primary citation | Hsieh, J.M.,Tsirulnikov, K.,Sawaya, M.R.,Magilnick, N.,Abuladze, N.,Kurtz, I.,Abramson, J.,Pushkin, A. Structures of aminoacylase 3 in complex with acetylated substrates. Proc.Natl.Acad.Sci.USA, 107:17962-17967, 2010 Cited by PubMed Abstract: 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(α)-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. PubMed: 20921362DOI: 10.1073/pnas.1006687107 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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