5A9Q

Human nuclear pore complex

Summary for 5A9Q

• Entry DOI: 10.2210/pdb5a9q/pdb
• EMDB information: 3103
• Descriptor: NUCLEOPORIN NUP43, NUCLEAR PORE COMPLEX PROTEIN NUP155, NUCLEAR PORE COMPLEX PROTEIN NUP160, ... (10 entities in total)
• Functional Keywords: transport protein
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Chromosome, centromere, kinetochore: Q8NFH3 Q8NFH4 Q96EE3; Nucleus, nuclear pore complex : O75694 Q12769 Q8WUM0 Q9BW27; Nucleus membrane : P57740; Nucleus membrane ; Peripheral membrane protein; Nucleoplasmic side : P52948; Cytoplasmic vesicle, COPII-coated vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : P55735
• Total number of polymer chains: 38
• Total formula weight: 3243761.45

Authors

von Appen, A.,Kosinski, J.,Sparks, L.,Ori, A.,DiGuilio, A.,Vollmer, B.,Mackmull, M.,Banterle, N.,Parca, L.,Kastritis, P.,Buczak, K.,Mosalaganti, S.,Hagen, W.,Andres-Pons, A.,Lemke, E.A.,Bork, P.,Antonin, W.,Glavy, J.S.,Bui, K.H.,Beck, M. (deposition date: 2015-07-22, release date: 2015-09-30, Last modification date: 2024-05-08)

Primary citation

Von Appen, A.,Kosinski, J.,Sparks, L.,Ori, A.,Diguilio, A.,Vollmer, B.,Mackmull, M.,Banterle, N.,Parca, L.,Kastritis, P.,Buczak, K.,Mosalaganti, S.,Hagen, W.,Andres-Pons, A.,Lemke, E.A.,Bork, P.,Antonin, W.,Glavy, J.S.,Bui, K.H.,Beck, M.
In Situ Structural Analysis of the Human Nuclear Pore Complex
Nature, 526:140-, 2015

PubMed Abstract: Nuclear pore complexes are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Determining their 110-megadalton structure imposes a formidable challenge and requires in situ structural biology approaches. Of approximately 30 nucleoporins (Nups), 15 are structured and form the Y and inner-ring complexes. These two major scaffolding modules assemble in multiple copies into an eight-fold rotationally symmetric structure that fuses the inner and outer nuclear membranes to form a central channel of ~60 nm in diameter. The scaffold is decorated with transport-channel Nups that often contain phenylalanine-repeat sequences and mediate the interaction with cargo complexes. Although the architectural arrangement of parts of the Y complex has been elucidated, it is unclear how exactly it oligomerizes in situ. Here we combine cryo-electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modelling to generate, to our knowledge, the most comprehensive architectural model of the human nuclear pore complex to date. Our data suggest previously unknown protein interfaces across Y complexes and to inner-ring complex members. We show that the transport-channel Nup358 (also known as Ranbp2) has a previously unanticipated role in Y-complex oligomerization. Our findings blur the established boundaries between scaffold and transport-channel Nups. We conclude that, similar to coated vesicles, several copies of the same structural building block--although compositionally identical--engage in different local sets of interactions and conformations.

PubMed: 26416747
DOI: 10.1038/NATURE15381

Experimental method

ELECTRON MICROSCOPY (23 Å)