1w4t

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[[Image:1w4t.gif|left|200px]]<br /><applet load="1w4t" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1w4t, resolution 1.950&Aring;" />
 
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'''X-RAY CRYSTALLOGRAPHIC STRUCTURE OF PSEUDOMONAS AERUGINOSA ARYLAMINE N-ACETYLTRANSFERASE'''<br />
 
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==Overview==
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==X-ray crystallographic structure of Pseudomonas aeruginosa arylamine N-acetyltransferase==
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<StructureSection load='1w4t' size='340' side='right'caption='[[1w4t]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9HUY3_PSEAE Q9HUY3_PSEAE]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w4/1w4t_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1w4t ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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<ref>PMID:15447630</ref>
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1W4T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4T OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15447630 15447630]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1w4t" style="background-color:#fffaf0;"></div>
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[[Category: Bhakta, S.]]
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[[Category: Dupret, J M.]]
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[[Category: Holton, S J.]]
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[[Category: Noble, M E.]]
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[[Category: Rodrigues-Lima, F.]]
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[[Category: Sim, E.]]
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[[Category: Westwood, I M.]]
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[[Category: SO4]]
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[[Category: 5-aminosalicylic acid]]
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[[Category: acyltransferase]]
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[[Category: arylamine n-acetyltransferase]]
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[[Category: nat]]
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[[Category: pseudomonas aeruginosa]]
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[[Category: xenobiotic metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:28 2008''
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==See Also==
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*[[Arylamine N-acetyltransferase 3D structures|Arylamine N-acetyltransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Bhakta S]]
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[[Category: Dupret J-M]]
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[[Category: Holton SJ]]
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[[Category: Noble ME]]
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[[Category: Rodrigues-Lima F]]
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[[Category: Sim E]]
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[[Category: Westwood IM]]

Current revision

X-ray crystallographic structure of Pseudomonas aeruginosa arylamine N-acetyltransferase

PDB ID 1w4t

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