3i5q

From Proteopedia

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

Structural highlights

3i5q is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.204Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NU170_YEAST Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP170 probably plays an important role in NPC assembly and organization. In addition it is required for chromosome transmission fidelity.^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element.,Whittle JR, Schwartz TU J Biol Chem. 2009 Oct 9;284(41):28442-52. Epub 2009 Aug 11. PMID:19674973^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Marelli M, Aitchison JD, Wozniak RW. Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p. J Cell Biol. 1998 Dec 28;143(7):1813-30. PMID:9864357
↑ Lusk CP, Makhnevych T, Marelli M, Aitchison JD, Wozniak RW. Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes. J Cell Biol. 2002 Oct 28;159(2):267-78. Epub 2002 Oct 28. PMID:12403813 doi:10.1083/jcb.200203079
↑ Makhnevych T, Lusk CP, Anderson AM, Aitchison JD, Wozniak RW. Cell cycle regulated transport controlled by alterations in the nuclear pore complex. Cell. 2003 Dec 26;115(7):813-23. PMID:14697200
↑ Kerscher O, Hieter P, Winey M, Basrai MA. Novel role for a Saccharomyces cerevisiae nucleoporin, Nup170p, in chromosome segregation. Genetics. 2001 Apr;157(4):1543-53. PMID:11290711
↑ Iouk T, Kerscher O, Scott RJ, Basrai MA, Wozniak RW. The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint. J Cell Biol. 2002 Dec 9;159(5):807-19. Epub 2002 Dec 9. PMID:12473689 doi:10.1083/jcb.200205068
↑ Whittle JR, Schwartz TU. Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element. J Biol Chem. 2009 Oct 9;284(41):28442-52. Epub 2009 Aug 11. PMID:19674973 doi:10.1074/jbc.M109.023580