1XKS

The crystal structure of the N-terminal domain of Nup133 reveals a beta-propeller fold common to several nucleoporins

Summary for 1XKS

• Entry DOI: 10.2210/pdb1xks/pdb
• Descriptor: Nuclear pore complex protein Nup133 (2 entities in total)
• Functional Keywords: beta-propeller, helical insertions, protein transport
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus, nuclear pore complex: Q8WUM0
• Total number of polymer chains: 1
• Total formula weight: 48798.43

Authors

Berke, I.C.,Boehmer, T.,Blobel, G.,Schwartz, T.U. (deposition date: 2004-09-29, release date: 2004-12-07, Last modification date: 2024-04-03)

Primary citation

Berke, I.C.,Boehmer, T.,Blobel, G.,Schwartz, T.U.
Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex.
J.Cell Biol., 167:591-597, 2004

PubMed Abstract: Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs) whose complex architecture is generated from a set of only approximately 30 proteins, termed nucleoporins. Here, we explore the domain structure of Nup133, a nucleoporin in a conserved NPC subcomplex that is crucial for NPC biogenesis and is believed to form part of the NPC scaffold. We show that human Nup133 contains two domains: a COOH-terminal domain responsible for its interaction with its subcomplex through Nup107; and an NH2-terminal domain whose crystal structure reveals a seven-bladed beta-propeller. The surface properties and conservation of the Nup133 beta-propeller suggest it may mediate multiple interactions with other proteins. Other beta-propellers are predicted in a third of all nucleoporins. These and several other repeat-based motifs appear to be major elements of nucleoporins, indicating a level of structural repetition that may conceptually simplify the assembly and disassembly of this huge protein complex.

PubMed: 15557116
DOI: 10.1083/jcb.200408109

Experimental method

X-RAY DIFFRACTION (2.35 Å)