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3I5Q

Nup170(aa1253-1502) at 2.2 A, S.cerevisiae

Summary for 3I5Q
Entry DOI10.2210/pdb3i5q/pdb
Related3I4R 3I5P
DescriptorNucleoporin NUP170 (2 entities in total)
Functional Keywordshelical stack, membrane, mrna transport, nuclear pore complex, nucleus, phosphoprotein, protein transport, translocation, transmembrane, transport
Biological sourceSaccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
Cellular locationNucleus, nuclear pore complex: P38181
Total number of polymer chains2
Total formula weight58558.99
Authors
Whittle, J.R.R.,Schwartz, T.U. (deposition date: 2009-07-06, release date: 2009-08-11, Last modification date: 2024-10-09)
Primary citationWhittle, J.R.,Schwartz, T.U.
Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element.
J.Biol.Chem., 284:28442-28452, 2009
Cited by
PubMed Abstract: The nuclear pore complex (NPC) constitutes one of the largest protein assemblies in the eukaryotic cell and forms the exclusive gateway to the nucleus. The stable, approximately 15-20-MDa scaffold ring of the NPC is built from two multiprotein complexes arranged around a central 8-fold axis. Here we present crystal structures of two large architectural units, yNup170(979-1502) and hNup107(658-925) x hNup133(517-1156), each a constituent of one of the two multiprotein complexes. Conservation of domain arrangement and of tertiary structure suggests that Nup157/170 and Nup133 derived from a common ancestor. Together with the previously established ancestral coatomer element (ACE1), these two elements constitute the major alpha-helical building blocks of the NPC scaffold and define its branched, lattice-like architecture, similar to vesicle coats like COPII. We hypothesize that the extant NPC evolved early during eukaryotic evolution from a rudimentary structure composed of several identical copies of a few ancestral elements, later diversified and specified by gene duplication.
PubMed: 19674973
DOI: 10.1074/jbc.M109.023580
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.204 Å)
Structure validation

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