2yb5: Difference between revisions
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< | ==Structure of the fusidic acid resistance protein FusC== | ||
<StructureSection load='2yb5' size='340' side='right'caption='[[2yb5]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2yb5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YB5 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]] 2.1Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2yb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yb5 OCA], [https://pdbe.org/2yb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yb5 RCSB], [https://www.ebi.ac.uk/pdbsum/2yb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yb5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/M1XHT1_STAAU M1XHT1_STAAU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Resistance to the antibiotic fusidic acid (FA) in the human pathogen Staphylococcus aureus usually results from expression of FusB-type proteins (FusB or FusC). These proteins bind to elongation factor G (EF-G), the target of FA, and rescue translation from FA-mediated inhibition by an unknown mechanism. Here we show that the FusB family are two-domain metalloproteins, the C-terminal domain of which contains a four-cysteine zinc finger with a unique structural fold. This domain mediates a high-affinity interaction with the C-terminal domains of EF-G. By binding to EF-G on the ribosome, FusB-type proteins promote the dissociation of stalled ribosomeEF-GGDP complexes that form in the presence of FA, thereby allowing the ribosomes to resume translation. Ribosome clearance by these proteins represents a highly unusual antibiotic resistance mechanism, which appears to be fine-tuned by the relative abundance of FusB-type protein, ribosomes, and EF-G. | |||
Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid.,Cox G, Thompson GS, Jenkins HT, Peske F, Savelsbergh A, Rodnina MV, Wintermeyer W, Homans SW, Edwards TA, O'Neill AJ Proc Natl Acad Sci U S A. 2012 Feb 7;109(6):2102-7. Epub 2012 Jan 20. PMID:22308410<ref>PMID:22308410</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
[[ | <div class="pdbe-citations 2yb5" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Cox | [[Category: Cox G]] | ||
[[Category: Edwards | [[Category: Edwards TA]] | ||
Latest revision as of 11:11, 23 August 2023
Structure of the fusidic acid resistance protein FusCStructure of the fusidic acid resistance protein FusC
Structural highlights
FunctionPublication Abstract from PubMedResistance to the antibiotic fusidic acid (FA) in the human pathogen Staphylococcus aureus usually results from expression of FusB-type proteins (FusB or FusC). These proteins bind to elongation factor G (EF-G), the target of FA, and rescue translation from FA-mediated inhibition by an unknown mechanism. Here we show that the FusB family are two-domain metalloproteins, the C-terminal domain of which contains a four-cysteine zinc finger with a unique structural fold. This domain mediates a high-affinity interaction with the C-terminal domains of EF-G. By binding to EF-G on the ribosome, FusB-type proteins promote the dissociation of stalled ribosomeEF-GGDP complexes that form in the presence of FA, thereby allowing the ribosomes to resume translation. Ribosome clearance by these proteins represents a highly unusual antibiotic resistance mechanism, which appears to be fine-tuned by the relative abundance of FusB-type protein, ribosomes, and EF-G. Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid.,Cox G, Thompson GS, Jenkins HT, Peske F, Savelsbergh A, Rodnina MV, Wintermeyer W, Homans SW, Edwards TA, O'Neill AJ Proc Natl Acad Sci U S A. 2012 Feb 7;109(6):2102-7. Epub 2012 Jan 20. PMID:22308410[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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