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PDBsum entry 3f3f

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Structural protein PDB id
3f3f
Contents
Protein chains
308 a.a.
475 a.a.

References listed in PDB file
Key reference
Title A fence-Like coat for the nuclear pore membrane.
Authors E.W.Debler, Y.Ma, H.S.Seo, K.C.Hsia, T.R.Noriega, G.Blobel, A.Hoelz.
Ref. Mol Cell, 2008, 32, 815-826. [DOI no: 10.1016/j.molcel.2008.12.001]
PubMed id 19111661
Abstract
We recently proposed a cylindrical coat for the nuclear pore membrane in the nuclear pore complex (NPC). This scaffold is generated by multiple copies of seven nucleoporins. Here, we report three crystal structures of the nucleoporin pair Seh1*Nup85, which is part of the coat cylinder. The Seh1*Nup85 assembly bears resemblance in its shape and dimensions to that of another nucleoporin pair, Sec13*Nup145C. Furthermore, the Seh1*Nup85 structures reveal a hinge motion that may facilitate conformational changes in the NPC during import of integral membrane proteins and/or during nucleocytoplasmic transport. We propose that Seh1*Nup85 and Sec13*Nup145C form 16 alternating, vertical rods that are horizontally linked by the three remaining nucleoporins of the coat cylinder. Shared architectural and mechanistic principles with the COPII coat indicate a common evolutionary origin and support the notion that the NPC coat represents another class of membrane coats.
Figure 2.
Figure 2. Detailed Structural Analysis of Nup85 and Seh1
(A) A ribbon representation of the Nup85 structure is shown in rainbow colors along the polypeptide chain from the N to the C terminus. The N-terminal domain invasion motif (DIM), the α-helical solenoid domain, and their secondary structure elements are indicated.
(B) The structure of the Seh1•Nup85 heterodimer. The Nup85^DIM (magenta), the Nup85 α-helical solenoid domain (blue), the Nup85 αQ-αR connector (red), the Seh1 β propeller (yellow), the disordered Seh1 5CD loop (gray dots), and the Seh1 2CD loop (orange) are indicated; a 90° rotated view is shown on the right. Dotted lines represent disordered regions.
(C) Schematic representation of the Seh1•Nup85 interaction. The Seh1 2CD loop, the Nup85 αQ-αR connector, and the DIM region are highlighted in orange, red, and pink, respectively.
(D) The β propeller domain of Seh1 in complex with the Nup85^DIM. Seh1 is shown in yellow, and the six blades are indicated. The Nup85^DIM contributes one strand to blade 6 and three strands to blade 7, completing the β propeller.
(E) Schematic representation of the Seh1 β propeller and its interaction with the Nup85^DIM.
Figure 5.
Figure 5. Flexibility of the Seh1•Nup85 Hetero-Octamer
(A) The hetero-octamers of crystal forms 1 and 2 are related by an vert, similar 35° hinge motion around the center of the hetero-octamer. On the right, a schematic of the two conformations is shown, where Seh1 and Nup85 are displayed as balls and cylinders, respectively.
(B) Crystal form 3 harbors a heterododecamer in the asymmetric unit (small ribbon representation). The two interfaces between the heterotetramers are identical. In the upper two neighboring heterotetramers of crystal form 3 (boxed in the heterododecamer), one heterotetramer is rotated by vert, similar 80° around its long axis with respect to crystal form 1. For clarity, a stripe of black lines marks the relative orientations of the heterotetramers. The alignment of the different structures was based on the lower heterotetramer of crystal form 1.
The above figures are reprinted by permission from Cell Press: Mol Cell (2008, 32, 815-826) copyright 2008.
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