title: Close identity between alternatively folded state N2 of ubiquitin and the conformation of the protein bound to the ubiquitin-activating enzyme.
abstract: We present the nuclear Overhauser effect-based structure determination of the Q41N variant of ubiquitin at 2500 bar, where the alternatively folded N2 state is 97% populated. This allows us to characterize the structure of the "pure" N2 state of ubiquitin. The N2 state shows a substantial change in the orientation of strand β5 compared to that of the normal folded N1 state, which matches the changes seen upon binding of ubiquitin to ubiquitin-activating enzyme E1. The recognition of E1 by ubiquitin is therefore best explained by conformational selection rather than induced-fit motion.
authors.affiliation: College of Pharmaceutical Sciences, Ritsumeikan University , Noji-higashi 1-1-1, Kusatsu 525-8577, Japan.
authors.forename: Soichiro
authors.initials: S
authors.lastname: Kitazawa
authors.forename: Tomoshi
authors.initials: T
authors.lastname: Kameda
authors.forename: Ayumi
authors.initials: A
authors.lastname: Kumo
authors.forename: Maho
authors.initials: M
authors.lastname: Yagi-Utsumi
authors.forename: Nicola J
authors.initials: NJ
authors.lastname: Baxter
authors.forename: Koichi
authors.initials: K
authors.lastname: Kato
authors.forename: Mike P
authors.initials: MP
authors.lastname: Williamson
authors.forename: Ryo
authors.initials: R
authors.lastname: Kitahara
mesh_terms: D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017510:Protein Folding; D025801:Ubiquitin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D044764:Ubiquitin-Activating Enzymes / Q000378:metabolism*
chemical_list: D025801:Ubiquitin; D044764:Ubiquitin-Activating Enzymes