6pu9: Difference between revisions
New page: '''Unreleased structure''' The entry 6pu9 is ON HOLD Authors: Kim, Y., Maltseva, N., Mulligan, R., Grimshaw, S., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (C... |
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==Crystal Structure of the Type B Chloramphenicol O-Acetyltransferase from Vibrio vulnificus== | |||
<StructureSection load='6pu9' size='340' side='right'caption='[[6pu9]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6pu9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_vulnificus_CMCP6 Vibrio vulnificus CMCP6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PU9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=6pu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pu9 OCA], [https://pdbe.org/6pu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pu9 RCSB], [https://www.ebi.ac.uk/pdbsum/6pu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pu9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A3Q0KYH6_VIBVU A0A3Q0KYH6_VIBVU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Chloramphenicol acetyltransferases (CATs) were among the first antibiotic resistance enzymes identified and have long been studied as model enzymes for examining plasmid-mediated antibiotic resistance. These enzymes acetylate the antibiotic chloramphenicol, which renders it incapable of inhibiting bacterial protein synthesis. CATs can be classified into different types: Type A CATs are known to be important for antibiotic resistance to chloramphenicol and fusidic acid. Type B CATs are often called xenobiotic acetyltransferases and adopt a similar structural fold to streptogramin acetyltransferases, which are known to be critical for streptogramin antibiotic resistance. Type C CATs have recently been identified and can also acetylate chloramphenicol, but their roles in antibiotic resistance are largely unknown. Here, we structurally and kinetically characterized three Vibrio CAT proteins from a nonpathogenic species (Aliivibrio fisheri) and two important human pathogens (Vibrio cholerae and Vibrio vulnificus). We found all three proteins, including one in a superintegron (V. cholerae), acetylated chloramphenicol, but did not acetylate aminoglycosides or dalfopristin. We also determined the 3D crystal structures of these CATs alone and in complex with crystal violet and taurocholate. These compounds are known inhibitors of Type A CATs, but have not been explored in Type B and Type C CATs. Based on sequence, structure, and kinetic analysis, we concluded that the V. cholerae and V. vulnificus CATs belong to the Type B class and the A. fisheri CAT belongs to the Type C class. Ultimately, our results provide a framework for studying the evolution of antibiotic resistance gene acquisition and chloramphenicol acetylation in Vibrio and other species. | |||
Structural and functional characterization of three Type B and C chloramphenicol acetyltransferases from Vibrio species.,Alcala A, Ramirez G, Solis A, Kim Y, Tan K, Luna O, Nguyen K, Vazquez D, Ward M, Zhou M, Mulligan R, Maltseva N, Kuhn ML Protein Sci. 2019 Nov 24. doi: 10.1002/pro.3793. PMID:31762145<ref>PMID:31762145</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6pu9" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Joachimiak | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Vibrio vulnificus CMCP6]] | |||
[[Category: Grimshaw S]] | |||
[[Category: Joachimiak A]] | |||
[[Category: Kim Y]] | |||
[[Category: Maltseva N]] | |||
[[Category: Mulligan R]] | |||
Latest revision as of 10:36, 11 October 2023
Crystal Structure of the Type B Chloramphenicol O-Acetyltransferase from Vibrio vulnificusCrystal Structure of the Type B Chloramphenicol O-Acetyltransferase from Vibrio vulnificus
Structural highlights
FunctionPublication Abstract from PubMedChloramphenicol acetyltransferases (CATs) were among the first antibiotic resistance enzymes identified and have long been studied as model enzymes for examining plasmid-mediated antibiotic resistance. These enzymes acetylate the antibiotic chloramphenicol, which renders it incapable of inhibiting bacterial protein synthesis. CATs can be classified into different types: Type A CATs are known to be important for antibiotic resistance to chloramphenicol and fusidic acid. Type B CATs are often called xenobiotic acetyltransferases and adopt a similar structural fold to streptogramin acetyltransferases, which are known to be critical for streptogramin antibiotic resistance. Type C CATs have recently been identified and can also acetylate chloramphenicol, but their roles in antibiotic resistance are largely unknown. Here, we structurally and kinetically characterized three Vibrio CAT proteins from a nonpathogenic species (Aliivibrio fisheri) and two important human pathogens (Vibrio cholerae and Vibrio vulnificus). We found all three proteins, including one in a superintegron (V. cholerae), acetylated chloramphenicol, but did not acetylate aminoglycosides or dalfopristin. We also determined the 3D crystal structures of these CATs alone and in complex with crystal violet and taurocholate. These compounds are known inhibitors of Type A CATs, but have not been explored in Type B and Type C CATs. Based on sequence, structure, and kinetic analysis, we concluded that the V. cholerae and V. vulnificus CATs belong to the Type B class and the A. fisheri CAT belongs to the Type C class. Ultimately, our results provide a framework for studying the evolution of antibiotic resistance gene acquisition and chloramphenicol acetylation in Vibrio and other species. Structural and functional characterization of three Type B and C chloramphenicol acetyltransferases from Vibrio species.,Alcala A, Ramirez G, Solis A, Kim Y, Tan K, Luna O, Nguyen K, Vazquez D, Ward M, Zhou M, Mulligan R, Maltseva N, Kuhn ML Protein Sci. 2019 Nov 24. doi: 10.1002/pro.3793. PMID:31762145[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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