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dc.contributor.authorKulczycka, Katarzyna
dc.contributor.authorDługosz, Maciej
dc.contributor.authorTrylska, Joanna
dc.identifier.citationKulczycka K, Długosz M, Trylska J. Molecular dynamics of ribosomal elongation factors G and Tu. European Biophysics Journal, 2011 Mar; 40(3):289-303. doi: 10.1007/s00249-010-0647-2
dc.identifier.otherDOI 10.1007/s00249-010-0647-2
dc.description.abstractTranslation on the ribosome is controlled by external factors. During polypeptide lengthening, elongation factors EF-Tu and EF-G consecutively interact with the bacterial ribosome. EF-Tu binds and delivers an aminoacyl-tRNA to the ribosomal A site and EF-G helps translocate the tRNAs between their binding sites after the peptide bond is formed. These processes occur at the expense of GTP. EF-Tu:tRNA and EF-G are of similar shape, share a common binding site, and undergo large conformational changes on interaction with the ribosome. To characterize the internal motion of these two elongation factors, we used 25 ns long all-atom molecular dynamics simulations. We observed enhanced mobility of EF-G domains III, IV, and V and of tRNA in the EF-Tu:tRNA complex. EF-Tu:GDP complex acquired a configuration different from that found in the crystal structure of EF-Tu with a GTP analogue, showing conformational changes in the switch I and II regions. The calculated electrostatic properties of elongation factors showed no global similarity even though matching electrostatic surface patches were found around the domain I that contacts the ribosome, and in the GDP/GTP binding region.en
dc.description.sponsorshipWe acknowledge support from the University of Warsaw (ICM BST 1255/2008, 1450/2009, 1550/2010 and G31-4), Polish Ministry of Science and Higher Education (N N301 245236), the Fogarty International Center (NIH Research Grant R03 TW07318), and the Foundation for Polish Science (Focus program and TEAM/2009-3/8—co-financed by European Regional Development Fund operated within Innovative Economy Operational Programme). KK is supported by the EU through the European Social Fund, contract 146 number UDA-POKL.04.01.01-00-072/09-00.en
dc.publisherSpringer Natureen
dc.rightsCreative Commons Uznanie autorstwa 3.0 Polskapl_PL
dc.titleMolecular dynamics of ribosomal elongation factors G and Tuen
dc.contributor.organizationInterdyscyplinarne Centrum Modelowania Matematycznego i Komputerowego, Uniwersytet Warszawskipl_PL
dc.description.epersonBartosz Brach

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Except where otherwise noted, this item's license is described as Creative Commons Uznanie autorstwa 3.0 Polska