<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Phillips-Jones MK</submitter><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>46180</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5387412</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>7</volume><pubmed_abstract>VanA-type resistance to glycopeptide antibiotics in clinical enterococci is regulated by the VanS&lt;sub>A&lt;/sub>R&lt;sub>A&lt;/sub> two-component signal transduction system. The nature of the molecular ligand that is recognised by the VanS&lt;sub>A&lt;/sub> sensory component has not hitherto been identified. Here we employ purified, intact and active VanS&lt;sub>A&lt;/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</pubmed_abstract><journal>Scientific reports</journal><pubmed_title>Hydrodynamics of the VanA-type VanS histidine kinase: an extended solution conformation and first evidence for interactions with vancomycin.</pubmed_title><pmcid>PMC5387412</pmcid><funding_grant_id>BB/M013081/1</funding_grant_id><funding_grant_id>BB/D001641/1</funding_grant_id><pubmed_authors>Hughes CS</pubmed_authors><pubmed_authors>Dinu V</pubmed_authors><pubmed_authors>Adams GG</pubmed_authors><pubmed_authors>Phillips-Jones MK</pubmed_authors><pubmed_authors>Gillis RB</pubmed_authors><pubmed_authors>Channell G</pubmed_authors><pubmed_authors>Kelsall CJ</pubmed_authors><pubmed_authors>Patching SG</pubmed_authors><pubmed_authors>Harding SE</pubmed_authors><pubmed_authors>Ashcroft AE</pubmed_authors></additional><is_claimable>false</is_claimable><name>Hydrodynamics of the VanA-type VanS histidine kinase: an extended solution conformation and first evidence for interactions with vancomycin.</name><description>VanA-type resistance to glycopeptide antibiotics in clinical enterococci is regulated by the VanS&lt;sub>A&lt;/sub>R&lt;sub>A&lt;/sub> two-component signal transduction system. The nature of the molecular ligand that is recognised by the VanS&lt;sub>A&lt;/sub> sensory component has not hitherto been identified. Here we employ purified, intact and active VanS&lt;sub>A&lt;/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</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Apr</publication><modification>2025-04-26T04:49:33.954Z</modification><creation>2019-03-27T02:41:01Z</creation></dates><accession>S-EPMC5387412</accession><cross_references><pubmed>28397853</pubmed><doi>10.1038/srep46180</doi></cross_references></HashMap>