1e2t

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{{Seed}}
 
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[[Image:1e2t.png|left|200px]]
 
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==Arylamine N-acetyltransferase (NAT) from Salmonella typhimurium==
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The line below this paragraph, containing "STRUCTURE_1e2t", creates the "Structure Box" on the page.
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<StructureSection load='1e2t' size='340' side='right'caption='[[1e2t]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1e2t]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E2T FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.8&#8491;</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=1e2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2t OCA], [https://pdbe.org/1e2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e2t RCSB], [https://www.ebi.ac.uk/pdbsum/1e2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2t ProSAT]</span></td></tr>
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{{STRUCTURE_1e2t| PDB=1e2t | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NHOA_SALTY NHOA_SALTY] Catalyzes both the acetyl-CoA-dependent N-acetylation of aromatic amines and the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the O-acetylation of N-hydroxy-Glu-P-1, and the N-acetylation of isoniazid and 2-aminofluorene.<ref>PMID:1569093</ref> <ref>PMID:7889864</ref>
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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/e2/1e2t_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=1e2t 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 ==
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Enzymes of the arylamine N-acetyltransferase (NAT) family are found in species ranging from Escherichia coli to humans. In humans they are known to be responsible for the acetylation of a number of arylamine and hydrazine drugs, and they are strongly linked to the carcinogenic potentiation of certain foreign substances. In prokaryotes their substrate specificities may vary and members of the gene family have been linked to pathways including amide synthesis during rifamycin production. Here we report the crystal structure at 2.8 A resolution of a representative member of this family from Salmonella typhimurium in the presence and absence of a covalently bound product analog. The structure reveals surprising mechanistic information including the presence of a Cys-His-Asp catalytic triad. The fold can be described in terms of three domains of roughly equal length with the second and third domains linked by an interdomain helix. The first two domains, a helical bundle and a beta-barrel, make up the catalytic triad using a structural motif identical to that of the cysteine protease superfamily.
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===ARYLAMINE N-ACETYLTRANSFERASE (NAT) FROM SALMONELLA TYPHIMURIUM===
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Structure of arylamine N-acetyltransferase reveals a catalytic triad.,Sinclair JC, Sandy J, Delgoda R, Sim E, Noble ME Nat Struct Biol. 2000 Jul;7(7):560-4. PMID:10876241<ref>PMID:10876241</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1e2t" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10876241}}, adds the Publication Abstract to the page
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*[[Arylamine N-acetyltransferase 3D structures|Arylamine N-acetyltransferase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10876241 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10876241}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1E2T is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2T OCA].
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Delgoda R]]
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==Reference==
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[[Category: Noble MEM]]
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<ref group="xtra">PMID:10876241</ref><references group="xtra"/>
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[[Category: Sandy J]]
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[[Category: N-hydroxyarylamine O-acetyltransferase]]
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[[Category: Sim E]]
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[[Category: Salmonella typhimurium]]
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[[Category: Sinclair JC]]
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[[Category: Delgoda, R.]]
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[[Category: Noble, M E.M.]]
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[[Category: Sandy, J.]]
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[[Category: Sim, E.]]
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[[Category: Sinclair, J C.]]
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[[Category: Acetyl coa dependent]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 03:55:55 2009''
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Current revision

Arylamine N-acetyltransferase (NAT) from Salmonella typhimurium

PDB ID 1e2t

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