5H1X

Crystal Structure of rat Nup62 Coiled-coil motif

Summary for 5H1X

• Entry DOI: 10.2210/pdb5h1x/pdb
• Descriptor: Nuclear pore glycoprotein p62 (2 entities in total)
• Functional Keywords: coiled-coil, structural protein
• Biological source: Rattus norvegicus (Rat)
• Cellular location: Nucleus, nuclear pore complex : P17955
• Total number of polymer chains: 3
• Total formula weight: 18609.05

Authors

Pravin, D. (deposition date: 2016-10-12, release date: 2017-10-04, Last modification date: 2023-11-08)

Primary citation

Dewangan, P.S.,Sonawane, P.J.,Chouksey, A.R.,Chauhan, R.
The Nup62 Coiled-Coil Motif Provides Plasticity for Triple-Helix Bundle Formation
Biochemistry, 56:2803-2811, 2017

PubMed Abstract: The central transport channel of the vertebrate nuclear pore complex (NPC) consists of nucleoporins: Nup62, Nup54, and Nup58. The coiled-coil domains in α-helical regions of these nucleoporins are thought to be crucial for several protein-protein interactions in the NPC subcomplexes. In this study, we determined the crystal structure of the coiled-coil domain of rat Nup62 fragment (residues 362-425) to 2.4 Å resolution. The crystal structure shows the conserved coiled-coil domain as a parallel three-helix bundle for the Nup62(362-425) fragment. On the basis of our size exclusion chromatography coupled to multiangle light scattering analysis and glutaraldehyde cross-linking experiments, we conclude that the Nup62(362-425) fragment displays dynamic behavior in solution and can also exist in either homodimeric or homotrimeric states. Our comparative analysis of the rat Nup62(362-425) homotrimeric structure with previously reported heterotrimeric structures [rat Nup62(362-425)·Nup54(346-407) and Xenopus Nup62(358-485)·Nup54(315-450)·Nup58(283-406) complexes] demonstrates the structural basis for parallel triple-helix bundle formation for Nup62 with different partners. Moreover, we show that the coiled-coil domain of Nup62 is sufficient for interaction with the coiled-coil domain of rat Exo70, a protein in an exocyst complex. On the basis of these observations, we suggest the plausible chain replacement mechanism that yields to diverse protein assemblies with Nup62. In summary, the coiled-coil motif present in Nup62 imparts the ability to form a homotrimer and heterotrimers either with Nup54 or with Nup54-Nup58 within the NPCs as well as with Exo70 beyond the NPCs. These complexes of Nup62 suggest the crucial role of the coiled-coil motifs in providing plasticity to various modular assemblies.

PubMed: 28406021
DOI: 10.1021/acs.biochem.6b01050

Experimental method

X-RAY DIFFRACTION (2.41 Å)