title: Structural basis of signal-sequence recognition by the signal recognition particle.
abstract: The signal recognition particle (SRP) recognizes and binds the signal sequence of nascent proteins as they emerge from the ribosome. We present here the 3.0-Å structure of a signal sequence bound to the Methanococcus jannaschii SRP core. Structural comparison with the free SRP core shows that signal-sequence binding induces formation of the GM-linker helix and a 180° flip of the NG domain-structural changes that ensure a hierarchical succession of events during protein targeting.
authors.affiliation: Department of Chemistry, Umeå University, Umeå, Sweden. tobias.hainzl@chem.umu.se
authors.forename: Tobias
authors.initials: T
authors.lastname: Hainzl
authors.forename: Shenghua
authors.initials: S
authors.lastname: Huang
authors.forename: Gitte
authors.initials: G
authors.lastname: Meriläinen
authors.forename: Kristoffer
authors.initials: K
authors.lastname: Brännström
authors.forename: A Elisabeth
authors.initials: AE
authors.lastname: Sauer-Eriksson
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D001483:Base Sequence; D018360:Crystallography, X-Ray; D017017:Methanococcus / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D021382:Protein Sorting Signals; D018271:Signal Recognition Particle / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D019843:Archaeal Proteins; D021382:Protein Sorting Signals; D018271:Signal Recognition Particle