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| ==Structure of CATI in complex with chloramphenicol== | | ==Structure of CATI in complex with chloramphenicol== |
| <StructureSection load='3u9f' size='340' side='right' caption='[[3u9f]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='3u9f' size='340' side='right'caption='[[3u9f]], [[Resolution|resolution]] 2.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3u9f]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U9F FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3u9f]] is a 18 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=3U9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U9F FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLM:CHLORAMPHENICOL'>CLM</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u9b|3u9b]]</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLM:CHLORAMPHENICOL'>CLM</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cat ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3u9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9f OCA], [https://pdbe.org/3u9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u9f RCSB], [https://www.ebi.ac.uk/pdbsum/3u9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9f ProSAT]</span></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9f OCA], [http://pdbe.org/3u9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u9f RCSB], [http://www.ebi.ac.uk/pdbsum/3u9f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9f ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/CAT_ECOLX CAT_ECOLX]] This enzyme is an effector of chloramphenicol resistance in bacteria. | | [https://www.uniprot.org/uniprot/CAT_ECOLX CAT_ECOLX] This enzyme is an effector of chloramphenicol resistance in bacteria. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Novel antibiotics are needed to overcome the challenge of continually evolving bacterial resistance. This has led to a renewed interest in mechanistic studies of once popular antibiotics like chloramphenicol (CAM). Chloramphenicol acetyltransferases (CATs) are enzymes that covalently modify CAM, rendering it inactive against its target, the ribosome, and thereby causing resistance to CAM. Out of the three major types of CAT (CAT(I-III) ), the CAM-specific CAT(III) has been studied extensively. Much less is known about another clinically important type, CAT(I) . In addition to inactivating CAM and unlike CAT(III) , CAT(I) confers resistance to a structurally distinct antibiotic, fusidic acid (FA). The origin of the broader substrate specificity of CAT(I) has not been fully elucidated. To understand the substrate binding features of CAT(I) , its crystal structures in the unbound (apo) and CAM-bound forms were determined. The analysis of these and previously determined CAT(I) -FA and CAT(III) -CAM structures revealed interactions responsible for CAT(I) binding to its substrates and clarified the broader substrate preference of CAT(I) compared to that of CAT(III) .
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| The structural basis for substrate versatility of chloramphenicol acetyltransferase CAT(I).,Biswas T, Houghton JL, Garneau-Tsodikova S, Tsodikov OV Protein Sci. 2012 Jan 31. doi: 10.1002/pro.2036. PMID:22294317<ref>PMID:22294317</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3u9f" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Chloramphenicol acetyltransferase|Chloramphenicol acetyltransferase]] | | *[[Chloramphenicol acetyltransferase 3D structures|Chloramphenicol acetyltransferase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus coli migula 1895]] | | [[Category: Escherichia coli]] |
| [[Category: Chloramphenicol O-acetyltransferase]] | | [[Category: Large Structures]] |
| [[Category: Biswas, T]] | | [[Category: Biswas T]] |
| [[Category: Garneau-Tsodikova, S]] | | [[Category: Garneau-Tsodikova S]] |
| [[Category: Tsodikov, O V]] | | [[Category: Tsodikov OV]] |
| [[Category: Acetylation of chloramphenicol]]
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| [[Category: Bacterial resistance]]
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| [[Category: Transferase-antibiotic complex]]
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