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PMID: 19576787 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture.

Structure (London, England : 1993) ·Vol. 17 ·No. 8 ·2009-08-12 ·Pages 1082-91

Leksa NC, Brohawn SG, Schwartz TU

Abstract

Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous protein assemblies residing in circular openings in the nuclear envelope. The NPC is modular, with transient and stable components. The stable core is essentially built from two multiprotein complexes, the Y-shaped heptameric Nup84 complex and the Nic96 complex, arranged around an eightfold axis. We present the crystal structure of Nup120(1-757), one of the two short arms of the Y-shaped Nup84 complex. The protein adopts a compact oval shape built around a novel bipartite alpha-helical domain intimately integrated with a beta-propeller domain. The domain arrangement is substantially different from the Nup85*Seh1 complex, which forms the other short arm of the Y. With the data presented here, we establish that all three branches of the Y-shaped Nup84 complex are tightly connected by helical interactions and that the beta-propellers likely form interaction site(s) to neighboring complexes.

MeSH Terms
Chromatography, Gel Crystallization Crystallography, X-Ray Green Fluorescent Proteins/genetics,metabolism Humans Microscopy, Fluorescence Models, Molecular Multiprotein Complexes/chemistry,metabolism Mutation Nuclear Pore/chemistry,metabolism Nuclear Pore Complex Proteins/chemistry,genetics,metabolism Nuclear Proteins/chemistry,genetics,metabolism Protein Binding Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Saccharomyces cerevisiae/genetics,metabolism Saccharomyces cerevisiae Proteins/chemistry,genetics,metabolism Static Electricity
Chemicals
Multiprotein Complexes NUP120 protein, S cerevisiae NUP145 protein, S cerevisiae NUP160 protein, human NUP85 protein, S cerevisiae Nuclear Pore Complex Proteins Nuclear Proteins Saccharomyces cerevisiae Proteins Green Fluorescent Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Leksa Nina C
Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Brohawn Stephen G
Schwartz Thomas U
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Article Info
Journal
Structure (London, England : 1993)
Abbr.
Structure
ISSN
1878-4186
DOI
10.1016/j.str.2009.06.003
Published
2009-08-12
Epub
2009-00-02
Pages
1082-91
Language
English
Region
United States
NLM ID
101087697
PMCID
PMC2743489
Subset
IM
Grants
NIGMS NIH HHS · R01 GM077537 · United States
NIGMS NIH HHS · R01 GM077537-03 · United States
NIGMS NIH HHS · GM77537 · United States
Databases
PDB
3HXR
Corrections
CommentIn
PMID: 19679081
External Links
PubMed source DOI: 10.1016/j.str.2009.06.003 PMC Full Text View journal details
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