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TitleStructural determinants and mechanism of mammalian CRM1 allostery.
Journal, issue, pagesStructure, Vol. 21, Issue 8, Page 1350-1360, Year 2013
Publish dateAug 6, 2013
AuthorsNicole Dölker / Clement E Blanchet / Béla Voß / David Haselbach / Christian Kappel / Thomas Monecke / Dmitri I Svergun / Holger Stark / Ralf Ficner / Ulrich Zachariae / Helmut Grubmüller / Achim Dickmanns /
PubMed AbstractProteins carrying nuclear export signals cooperatively assemble with the export factor CRM1 and the effector protein RanGTP. In lower eukaryotes, this cooperativity is coupled to CRM1 conformational ...Proteins carrying nuclear export signals cooperatively assemble with the export factor CRM1 and the effector protein RanGTP. In lower eukaryotes, this cooperativity is coupled to CRM1 conformational changes; however, it is unknown if mammalian CRM1 maintains its compact conformation or shows similar structural flexibility. Here, combinations of small-angle X-ray solution scattering and electron microscopy experiments with molecular dynamics simulations reveal pronounced conformational flexibility in mammalian CRM1 and demonstrate that RanGTP binding induces association of its N- and C-terminal regions to form a toroid structure. The CRM1 toroid is stabilized mainly by local interactions between the terminal regions, rather than by global strain. The CRM1 acidic loop is key in transmitting the effect of this RanGTP-induced global conformational change to the NES-binding cleft by shifting its population to the open state, which displays enhanced cargo affinity. Cooperative CRM1 export complex assembly thus constitutes a highly dynamic process, encompassing an intricate interplay of global and local structural changes.
External linksStructure / PubMed:23850451
MethodsSAS (X-ray synchrotron) / EM (single particle)
Resolution20.0 Å
Structure data

SASDAJ4:
CRM1 (Exportin-1)
Method: SAXS/SANS

SASDAK4:
CRM1 RanGTP (Exportin-1 + GTP-binding nuclear protein Ran)
Method: SAXS/SANS

SASDAL4:
CRM1 RanGTP Snu1 (Exportin-1 + GTP-binding nuclear protein Ran + Snurportin-1)
Method: SAXS/SANS

SASDAM4:
CRM1 Snu1 (Exportin-1 + Snurportin-1)
Method: SAXS/SANS

EMDB-2274:
human crm1 extended conformation
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-5564:
Compact conformation of human crm1
Method: EM (single particle) / Resolution: 20.0 Å

Source
  • Mus musculus (house mouse)
  • Homo sapiens (human)

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