2yb5: Difference between revisions

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<StructureSection load='2yb5' size='340' side='right'caption='[[2yb5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='2yb5' size='340' side='right'caption='[[2yb5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2yb5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YB5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2yb5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yb5 OCA], [http://pdbe.org/2yb5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yb5 RCSB], [http://www.ebi.ac.uk/pdbsum/2yb5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yb5 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=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>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">

Revision as of 18:03, 17 November 2021

Structure of the fusidic acid resistance protein FusCStructure of the fusidic acid resistance protein FusC

Structural highlights

2yb5 is a 2 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Cox G, Thompson GS, Jenkins HT, Peske F, Savelsbergh A, Rodnina MV, Wintermeyer W, Homans SW, Edwards TA, O'Neill AJ. Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid. Proc Natl Acad Sci U S A. 2012 Feb 7;109(6):2102-7. Epub 2012 Jan 20. PMID:22308410 doi:10.1073/pnas.1117275109

2yb5, resolution 2.10Å

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OCA