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3u9b

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Current revision (10:18, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3u9b' size='340' side='right'caption='[[3u9b]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='3u9b' size='340' side='right'caption='[[3u9b]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3u9b]] is a 9 chain structure with sequence from [https://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=3U9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U9B FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3u9b]] is a 9 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=3U9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U9B FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3u9f|3u9f]]</div></td></tr>
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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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cat ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chloramphenicol_O-acetyltransferase Chloramphenicol O-acetyltransferase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3u9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9b OCA], [https://pdbe.org/3u9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u9b RCSB], [https://www.ebi.ac.uk/pdbsum/3u9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9b ProSAT]</span></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=3u9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9b OCA], [https://pdbe.org/3u9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u9b RCSB], [https://www.ebi.ac.uk/pdbsum/3u9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9b ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CAT_ECOLX CAT_ECOLX]] This enzyme is an effector of chloramphenicol resistance in bacteria.
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[https://www.uniprot.org/uniprot/CAT_ECOLX CAT_ECOLX] This enzyme is an effector of chloramphenicol resistance in bacteria.
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<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&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 3u9b" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Chloramphenicol acetyltransferase 3D structures|Chloramphenicol acetyltransferase 3D structures]]
*[[Chloramphenicol acetyltransferase 3D structures|Chloramphenicol acetyltransferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
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[[Category: Chloramphenicol O-acetyltransferase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Biswas, T]]
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[[Category: Biswas T]]
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[[Category: Garneau-Tsodikova, S]]
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[[Category: Garneau-Tsodikova S]]
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[[Category: Tsodikov, O V]]
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[[Category: Tsodikov OV]]
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[[Category: Acetyltransferase]]
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[[Category: Chrolamphenicol resistance]]
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[[Category: Transferase]]
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Current revision

Structure of apo-CATI

PDB ID 3u9b

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