{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Phillips-Jones MK"],"funding":["Biotechnology and Biological Sciences Research Council"],"pagination":["46180"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5387412"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7"],"pubmed_abstract":["VanA-type resistance to glycopeptide antibiotics in clinical enterococci is regulated by the VanS<sub>A</sub>R<sub>A</sub> two-component signal transduction system. The nature of the molecular ligand that is recognised by the VanS<sub>A</sub> sensory component has not hitherto been identified. Here we employ purified, intact and active VanS<sub>A</sub> membrane protein (henceforth referred to as VanS) in analytical ultracentrifugation experiments to study VanS oligomeric state and conformation in the absence and presence of vancomycin. A combination of sedimentation velocity and sedimentation equilibrium in the analytical ultracentrifuge (SEDFIT, SEDFIT-MSTAR and MULTISIG analysis) showed that VanS in the absence of the ligand is almost entirely monomeric (molar mass M = 45.7 kDa) in dilut"],"journal":["Scientific reports"],"pubmed_title":["Hydrodynamics of the VanA-type VanS histidine kinase: an extended solution conformation and first evidence for interactions with vancomycin."],"pmcid":["PMC5387412"],"funding_grant_id":["BB/M013081/1","BB/D001641/1"],"pubmed_authors":["Hughes CS","Dinu V","Adams GG","Phillips-Jones MK","Gillis RB","Channell G","Kelsall CJ","Patching SG","Harding SE","Ashcroft AE"],"additional_accession":[]},"is_claimable":false,"name":"Hydrodynamics of the VanA-type VanS histidine kinase: an extended solution conformation and first evidence for interactions with vancomycin.","description":"VanA-type resistance to glycopeptide antibiotics in clinical enterococci is regulated by the VanS<sub>A</sub>R<sub>A</sub> two-component signal transduction system. The nature of the molecular ligand that is recognised by the VanS<sub>A</sub> sensory component has not hitherto been identified. Here we employ purified, intact and active VanS<sub>A</sub> membrane protein (henceforth referred to as VanS) in analytical ultracentrifugation experiments to study VanS oligomeric state and conformation in the absence and presence of vancomycin. A combination of sedimentation velocity and sedimentation equilibrium in the analytical ultracentrifuge (SEDFIT, SEDFIT-MSTAR and MULTISIG analysis) showed that VanS in the absence of the ligand is almost entirely monomeric (molar mass M = 45.7 kDa) in dilut","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Apr","modification":"2025-04-26T04:49:33.954Z","creation":"2019-03-27T02:41:01Z"},"accession":"S-EPMC5387412","cross_references":{"pubmed":["28397853"],"doi":["10.1038/srep46180"]}}