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3F7F

Structure of Nup120

Summary for 3F7F
Entry DOI10.2210/pdb3f7f/pdb
DescriptorNucleoporin NUP120, MERCURY (II) ION (2 entities in total)
Functional Keywordsnucleoporin, nuclear pore complex, macromolecular assembly, membrane coat, nucleocytoplasmic transport, beta-propeller, alpha-helical solenoid domain, coiled coil, mrna transport, nucleus, protein transport, translocation, structural protein
Biological sourceSaccharomyces cerevisiae
Cellular locationNucleus, nuclear pore complex: P35729
Total number of polymer chains4
Total formula weight337929.80
Authors
Seo, H.S.,Ma, Y.,Debler, E.W.,Blobel, G.,Hoelz, A. (deposition date: 2008-11-08, release date: 2009-08-18, Last modification date: 2023-12-27)
Primary citationSeo, H.S.,Ma, Y.,Debler, E.W.,Wacker, D.,Kutik, S.,Blobel, G.,Hoelz, A.
Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex.
Proc.Natl.Acad.Sci.USA, 106:14281-14286, 2009
Cited by
PubMed Abstract: The Nup84 complex constitutes a key building block in the nuclear pore complex (NPC). Here we present the crystal structure of one of its 7 components, Nup120, which reveals a beta propeller and an alpha-helical domain representing a novel fold. We discovered a previously unidentified interaction of Nup120 with Nup133 and confirmed the physiological relevance in vivo. As mapping of the individual components in the Nup84 complex places Nup120 and Nup133 at opposite ends of the heptamer, our findings indicate a head-to-tail arrangement of elongated Nup84 complexes into a ring structure, consistent with a fence-like coat for the nuclear pore membrane. The attachment site for Nup133 lies at the very end of an extended unstructured region, which allows for flexibility in the diameter of the Nup84 complex ring. These results illuminate important roles of terminal unstructured segments in nucleoporins for the architecture, function, and assembly of the NPC.
PubMed: 19706512
DOI: 10.1073/pnas.0907453106
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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数据于2025-06-18公开中

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