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2cla

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[[Image:2cla.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THE ASP-199-ASN MUTANT OF CHLORAMPHENICOL ACETYLTRANSFERASE TO 2.35 ANGSTROMS RESOLUTION. STRUCTURAL CONSEQUENCES OF DISRUPTION OF A BURIED SALT-BRIDGE==
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|PDB= 2cla |SIZE=350|CAPTION= <scene name='initialview01'>2cla</scene>, resolution 2.35&Aring;
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<StructureSection load='2cla' size='340' side='right'caption='[[2cla]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>
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<table><tr><td colspan='2'>[[2cla]] 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=2CLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CLA FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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]] 2.35&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr>
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|DOMAIN=
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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=2cla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cla OCA], [https://pdbe.org/2cla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cla RCSB], [https://www.ebi.ac.uk/pdbsum/2cla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cla ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cla OCA], [http://www.ebi.ac.uk/pdbsum/2cla PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cla RCSB]</span>
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== Function ==
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}}
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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/2cla_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=2cla ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF THE ASP-199-ASN MUTANT OF CHLORAMPHENICOL ACETYLTRANSFERASE TO 2.35 ANGSTROMS RESOLUTION. STRUCTURAL CONSEQUENCES OF DISRUPTION OF A BURIED SALT-BRIDGE'''
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==See Also==
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*[[Chloramphenicol acetyltransferase 3D structures|Chloramphenicol acetyltransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structure of the Asp-199----Asn mutant of chloramphenicol acetyltransferase (CAT) has been determined to 2.35-A resolution. In wild-type CAT Asp-199 is involved in a fully buried intrasubunit salt bridge with Arg-18, an interaction that is adjacent to the active site. Replacement of aspartate with asparagine by site-directed mutagenesis disrupts this salt bridge and causes extensive conformational changes within the active site. The imidazole group of the catalytically essential His-195 is reoriented, with the loss of interactions thought to stabilize the preferred tautomer of this residue. Arg-18 and Asn-199 form three new intersubunit interactions as a result of large side-chain torsion angle changes which cause the movement of two polypeptide loops, some residues of which are up to 20 A away from the site of the mutation. The new interactions of Arg-18 and Asn-199 compensate for the loss of the buried salt bridge and afford near-wild-type thermostability to Asn-199 CAT, albeit with a greatly reduced activity.
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==About this Structure==
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2CLA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CLA OCA].
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==Reference==
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Crystal structure of the aspartic acid-199----asparagine mutant of chloramphenicol acetyltransferase to 2.35-A resolution: structural consequences of disruption of a buried salt bridge., Gibbs MR, Moody PC, Leslie AG, Biochemistry. 1990 Dec 25;29(51):11261-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2271709 2271709]
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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: Gibbs, M R.]]
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[[Category: Gibbs MR]]
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[[Category: Leslie, A G.W.]]
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[[Category: Leslie AGW]]
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[[Category: Moody, P C.E.]]
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[[Category: Moody PCE]]
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[[Category: transferase (acyltransferase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:23:03 2008''
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Current revision

CRYSTAL STRUCTURE OF THE ASP-199-ASN MUTANT OF CHLORAMPHENICOL ACETYLTRANSFERASE TO 2.35 ANGSTROMS RESOLUTION. STRUCTURAL CONSEQUENCES OF DISRUPTION OF A BURIED SALT-BRIDGE

PDB ID 2cla

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