5cfs: Difference between revisions
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<StructureSection load='5cfs' size='340' side='right'caption='[[5cfs]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5cfs' size='340' side='right'caption='[[5cfs]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5cfs]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5cfs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CFS FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene>, <scene name='pdbligand=TOY:TOBRAMYCIN'>TOY</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene>, <scene name='pdbligand=TOY:TOBRAMYCIN'>TOY</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=5cfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cfs OCA], [https://pdbe.org/5cfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cfs RCSB], [https://www.ebi.ac.uk/pdbsum/5cfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cfs ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6X3H6_PSEAI Q6X3H6_PSEAI] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: | [[Category: Bassenden AV]] | ||
[[Category: | [[Category: Berghuis AM]] | ||
[[Category: | [[Category: Rodionov D]] | ||
Latest revision as of 15:03, 14 June 2023
Crystal Structure of ANT(2")-Ia in complex with AMPCPP and tobramycinCrystal Structure of ANT(2")-Ia in complex with AMPCPP and tobramycin
Structural highlights
FunctionPublication Abstract from PubMedWidespread use and misuse of antibiotics has allowed for the selection of resistant bacteria capable of avoiding the effects of antibiotics. The primary mechanism for resistance to aminoglycosides, a broad-spectrum class of antibiotics, is through covalent enzymatic modification of the drug, waning their bactericidal effect. Tobramycin and gentamicin are two medically important aminoglycosides targeted by several different resistance factors, including aminoglycoside 2-nucleotidyltransferase [ANT(2)], the primary cause of aminoglycoside resistance in North America. We describe here two crystal structures of ANT(2), each in complex with AMPCPP, Mn2+, and either tobramycin or gentamicin. Together these structures outline ANT(2)'s specificity for clinically used substrates. Importantly, these structures complete our structural knowledge for the set of enzymes that most frequently confer clinically observed resistance to tobramycin and gentamicin. Comparison of tobramycin and gentamicin binding to enzymes in this resistome, as well as to the intended target, the bacterial ribosome, reveals surprising diversity in observed drug-target interactions. Analysis of the diverse binding modes informs that there are limited opportunities for developing aminoglycoside analogs capable of evading resistance. Structural Analysis of the Tobramycin and Gentamicin Clinical Resistome Reveals Limitations for Next-generation Aminoglycoside Design.,Bassenden AV, Rodionov D, Shi K, Berghuis AM ACS Chem Biol. 2016 Mar 4. PMID:26900880[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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