3cla

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(New page: 200px<br /><applet load="3cla" size="450" color="white" frame="true" align="right" spinBox="true" caption="3cla, resolution 1.75&Aring;" /> '''REFINED CRYSTAL STRU...)
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[[Image:3cla.gif|left|200px]]<br /><applet load="3cla" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="3cla, resolution 1.75&Aring;" />
 
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'''REFINED CRYSTAL STRUCTURE OF TYPE III CHLORAMPHENICOL ACETYLTRANSFERASE AT 1.75 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==REFINED CRYSTAL STRUCTURE OF TYPE III CHLORAMPHENICOL ACETYLTRANSFERASE AT 1.75 ANGSTROMS RESOLUTION==
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High level bacterial resistance to chloramphenicol is generally due to, O-acetylation of the antibiotic in a reaction catalysed by chloramphenicol, acetyltransferase (CAT, EC 2.3.1.28) in which acetyl-coenzyme A is the, acyl donor. The crystal structure of the type III enzyme from Escherichia, coli with chloramphenicol bound has been determined and refined at 1.75 A, resolution, using a restrained parameter reciprocal space least squares, procedure. The refined model, which includes chloramphenicol, 204 solvent, molecules and two cobalt ions has a crystallographic R-factor of 18.3% for, 27,300 reflections between 6 and 1.75 A resolution. The root-mean-square, deviation in bond lengths from ideal values is 0.02 A. The cobalt ions, play a crucial role in stabilizing the packing of the molecule in the, crystal lattice. CAT is a trimer of identical subunits (monomer Mr 25,000), and the trimeric structure is stabilized by a number of hydrogen bonds, some of which result in the extension of a beta-sheet across the subunit, interface. Chloramphenicol binds in a deep pocket located at the boundary, between adjacent subunits of the trimer, such that the majority of, residues forming the binding pocket belong to one subunit while the, catalytically essential histidine belongs to the adjacent subunit. His195, is appropriately positioned to act as a general base catalyst in the, reaction, and the required tautomeric stabilization is provided by an, unusual interaction with a main-chain carbonyl oxygen.
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<StructureSection load='3cla' size='340' side='right'caption='[[3cla]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3cla]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CLA 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]] 1.75&#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=CO:COBALT+(II)+ION'>CO</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=3cla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cla OCA], [https://pdbe.org/3cla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cla RCSB], [https://www.ebi.ac.uk/pdbsum/3cla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cla ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAT3_ECOLX CAT3_ECOLX] This enzyme is an effector of chloramphenicol resistance in bacteria.
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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/cl/3cla_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=3cla ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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3CLA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CO and CLM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chloramphenicol_O-acetyltransferase Chloramphenicol O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.28 2.3.1.28] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3CLA OCA].
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*[[Chloramphenicol acetyltransferase|Chloramphenicol acetyltransferase]]
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*[[Chloramphenicol acetyltransferase 3D structures|Chloramphenicol acetyltransferase 3D structures]]
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==Reference==
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__TOC__
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Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75 A resolution., Leslie AG, J Mol Biol. 1990 May 5;213(1):167-86. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2187098 2187098]
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</StructureSection>
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[[Category: Chloramphenicol O-acetyltransferase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Leslie, A.G.W.]]
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[[Category: Leslie AGW]]
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[[Category: CLM]]
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[[Category: CO]]
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[[Category: transferase (acyltransferase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:35:06 2007''
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Current revision

REFINED CRYSTAL STRUCTURE OF TYPE III CHLORAMPHENICOL ACETYLTRANSFERASE AT 1.75 ANGSTROMS RESOLUTION

PDB ID 3cla

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