2xat

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(New page: 200px<br /><applet load="2xat" size="450" color="white" frame="true" align="right" spinBox="true" caption="2xat, resolution 3.20&Aring;" /> '''COMPLEX OF THE HEXAP...)
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[[Image:2xat.jpg|left|200px]]<br /><applet load="2xat" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2xat, resolution 3.20&Aring;" />
 
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'''COMPLEX OF THE HEXAPEPTIDE XENOBIOTIC ACETYLTRANSFERASE WITH CHLORAMPHENICOL AND DESULFO-COENZYME A'''<br />
 
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==Overview==
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==COMPLEX OF THE HEXAPEPTIDE XENOBIOTIC ACETYLTRANSFERASE WITH CHLORAMPHENICOL AND DESULFO-COENZYME A==
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The crystal structure of the xenobiotic acetyltransferase from Pseudomonas, aeruginosa PA103 (PaXAT) has been determined, as well as that of its, complex with the substrate chloramphenicol and the cofactor analogue, desulfo-coenzyme A. PaXAT is a member of the large hexapeptide, acyltransferase family of enzymes that display tandem repeated copies of a, six-residue hexapeptide repeat sequence motif encoding a left-handed, parallel beta helix (L betaH) structural domain. The xenobiotic, acetyltransferase class of hexapeptide acyltransferases is composed of, microbial enzymes that utilize acetyl-CoA to acylate a variety of, hydroxyl-bearing acceptors. The active site of trimeric PaXAT is a short, tunnel into which chloramphenicol and the cofactor analogue desulfo-CoA, project from opposite ends. This tunnel is formed by the flat parallel, beta sheets of two separate L betaH domains and an extended 39-residue, loop. His 79 of the extended loop forms hydrogen bonds from its imidazole, NE2 atom to the 3-hydroxyl group of chloramphenicol and from its ND1 group, to the peptide oxygen of Thr 86. The interactions of this histidine, residue are similar to those found in the structurally unrelated type III, chloramphenicol acetyltransferase and suggest that His 79 of PaXAT may be, similarly positioned and tautomerically stabilized to serve as a general, base catalyst.
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<StructureSection load='2xat' size='340' side='right'caption='[[2xat]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2xat]] 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=2XAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XAT FirstGlance]. <br>
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2XAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with CLM and DCA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2XAT OCA].
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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]] 3.2&#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=CLM:CHLORAMPHENICOL'>CLM</scene>, <scene name='pdbligand=DCA:DESULFO-COENZYME+A'>DCA</scene></td></tr>
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==Reference==
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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=2xat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xat OCA], [https://pdbe.org/2xat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xat RCSB], [https://www.ebi.ac.uk/pdbsum/2xat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xat ProSAT]</span></td></tr>
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Structure of the hexapeptide xenobiotic acetyltransferase from Pseudomonas aeruginosa., Beaman TW, Sugantino M, Roderick SL, Biochemistry. 1998 May 12;37(19):6689-96. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9578552 9578552]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAT4_PSEAE CAT4_PSEAE] This enzyme is an effector of chloramphenicol (Cm) resistance in bacteria. Acetylates Cm but not 1-acetoxy-Cm.
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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/xa/2xat_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=2xat ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Beaman TW]]
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[[Category: Beaman, T.W.]]
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[[Category: Roderick SL]]
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[[Category: Roderick, S.L.]]
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[[Category: Sugantino M]]
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[[Category: Sugantino, M.]]
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[[Category: CLM]]
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[[Category: DCA]]
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[[Category: acetyltransferase]]
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[[Category: chloramphenicol]]
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[[Category: left-handed beta helix]]
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[[Category: xenobiotic]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:29:56 2007''
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Current revision

COMPLEX OF THE HEXAPEPTIDE XENOBIOTIC ACETYLTRANSFERASE WITH CHLORAMPHENICOL AND DESULFO-COENZYME A

PDB ID 2xat

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