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| | <StructureSection load='1w4t' size='340' side='right'caption='[[1w4t]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='1w4t' size='340' side='right'caption='[[1w4t]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1w4t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1W4T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1w4t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W4T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.95Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA4827 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1w4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w4t OCA], [http://pdbe.org/1w4t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w4t RCSB], [http://www.ebi.ac.uk/pdbsum/1w4t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w4t ProSAT]</span></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=1w4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w4t OCA], [https://pdbe.org/1w4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w4t RCSB], [https://www.ebi.ac.uk/pdbsum/1w4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w4t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9HUY3_PSEAE Q9HUY3_PSEAE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bhakta, S]] | |
| - | [[Category: Dupret, J M]] | |
| - | [[Category: Holton, S J]] | |
| - | [[Category: Noble, M E]] | |
| - | [[Category: Rodrigues-Lima, F]] | |
| - | [[Category: Sim, E]] | |
| - | [[Category: Westwood, I M]] | |
| - | [[Category: 5- aminosalicylic acid]] | |
| - | [[Category: Acyltransferase]] | |
| - | [[Category: Arylamine n-acetyltransferase]] | |
| - | [[Category: Nat]] | |
| | [[Category: Pseudomonas aeruginosa]] | | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Transferase]] | + | [[Category: Bhakta S]] |
| - | [[Category: Xenobiotic metabolism]] | + | [[Category: Dupret J-M]] |
| | + | [[Category: Holton SJ]] |
| | + | [[Category: Noble ME]] |
| | + | [[Category: Rodrigues-Lima F]] |
| | + | [[Category: Sim E]] |
| | + | [[Category: Westwood IM]] |
| Structural highlights
Function
Q9HUY3_PSEAE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The gene for NAT (arylamine N-acetyltransferase) from Pseudomonas aeruginosa (panat) has been cloned from genomic DNA, and the gene product (PANAT) expressed as an N-terminal histidine-tagged protein in Escherichia coli and purified via nickel ion affinity chromatography. The specific activities of PANAT against a broad range of substrates have been investigated and compared with those of other prokaryotic NAT enzymes. For most arylamine substrates identified, PANAT exhibits in vitro specific activities typically one order of magnitude greater than those of recombinant NAT enzymes from Mycobacterium smegmatis or Salmonella typhimurium. Among the substrates of PANAT so far identified are the anti-tubercular drug isoniazid, 5-aminosalicylate (a drug used in the treatment of inflammatory bowel disease), as well as important environmental pollutants such as 3,4-dichloroaniline and 2-aminofluorene. As well as acetylating common NAT substrates, PANAT is unique among the prokaryotic NATs so far studied in acetylating the folate precursor 4-aminobenzoic acid and the folate catabolite 4-aminobenzoylglutamate. The recombinant protein has been expressed in sufficient quantity to allow protein crystallization, and we have subsequently determined the 1.95 A structure of PANAT by X-ray crystallography.
Expression, purification, characterization and structure of Pseudomonas aeruginosa arylamine N-acetyltransferase.,Westwood IM, Holton SJ, Rodrigues-Lima F, Dupret JM, Bhakta S, Noble ME, Sim E Biochem J. 2005 Jan 15;385(Pt 2):605-12. PMID:15447630[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Westwood IM, Holton SJ, Rodrigues-Lima F, Dupret JM, Bhakta S, Noble ME, Sim E. Expression, purification, characterization and structure of Pseudomonas aeruginosa arylamine N-acetyltransferase. Biochem J. 2005 Jan 15;385(Pt 2):605-12. PMID:15447630 doi:10.1042/BJ20041330
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