Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for cooperativity of CRM1 export complex formation.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 110, Issue 3, Page 960-965, Year 2013
Publish date	Jan 15, 2013
Authors	Thomas Monecke / David Haselbach / Béla Voß / Andreas Russek / Piotr Neumann / Emma Thomson / Ed Hurt / Ulrich Zachariae / Holger Stark / Helmut Grubmüller / Achim Dickmanns / Ralf Ficner /
PubMed Abstract	In eukaryotes, the nucleocytoplasmic transport of macromolecules is mainly mediated by soluble nuclear transport receptors of the karyopherin-β superfamily termed importins and exportins. The highly ...In eukaryotes, the nucleocytoplasmic transport of macromolecules is mainly mediated by soluble nuclear transport receptors of the karyopherin-β superfamily termed importins and exportins. The highly versatile exportin chromosome region maintenance 1 (CRM1) is essential for nuclear depletion of numerous structurally and functionally unrelated protein and ribonucleoprotein cargoes. CRM1 has been shown to adopt a toroidal structure in several functional transport complexes and was thought to maintain this conformation throughout the entire nucleocytoplasmic transport cycle. We solved crystal structures of free CRM1 from the thermophilic eukaryote Chaetomium thermophilum. Surprisingly, unbound CRM1 exhibits an overall extended and pitched superhelical conformation. The two regulatory regions, namely the acidic loop and the C-terminal α-helix, are dramatically repositioned in free CRM1 in comparison with the ternary CRM1-Ran-Snurportin1 export complex. Single-particle EM analysis demonstrates that, in a noncrystalline environment, free CRM1 exists in equilibrium between extended, superhelical and compact, ring-like conformations. Molecular dynamics simulations show that the C-terminal helix plays an important role in regulating the transition from an extended to a compact conformation and reveal how the binding site for nuclear export signals of cargoes is modulated by different CRM1 conformations. Combining these results, we propose a model for the cooperativity of CRM1 export complex assembly involving the long-range allosteric communication between the distant binding sites of GTP-bound Ran and cargo.
External links	Proc Natl Acad Sci U S A / PubMed:23277578 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.941 - 18.0 Å
Structure data	EMDB-2110: Negative structure of open and closed conformation of crm1 Method: EM (single particle) / Resolution: 18.0 Å EMDB-2111: Negative structure of closed conformation of crm1 Method: EM (single particle) / Resolution: 18.0 Å PDB-4fgv: Crystal structure of free CRM1 (crystal form 1) Method: X-RAY DIFFRACTION / Resolution: 2.941 Å PDB-4hzk: Crystal structure of free CRM1 (crystal form 2) Method: X-RAY DIFFRACTION / Resolution: 3.1 Å
Source	Chaetomium thermophilum (fungus) chaetomium thermophilum var. thermophilum dsm 1495 (fungus) chaetomium thermophilum var. thermophilum (fungus)
Keywords	TRANSPORT PROTEIN / HEAT repeat protein / Importin-beta superfamily / Nuclear export of numerous protein and RNP cargoes / Nuclear export receptor