5TQB

Crystal structure of assembly chaperone of ribosomal protein L4 (Acl4) in complex with ribosomal protein L4 (RpL4)

Summary for 5TQB

• Entry DOI: 10.2210/pdb5tqb/pdb
• Descriptor: 60S ribosomal protein L4-like protein, Assembly chaperone of ribosomal protein L4 (Acl4), 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: ribosome assembly chaperone, ribosomal protein
• Biological source: Chaetomium thermophilum; More
• Total number of polymer chains: 2
• Total formula weight: 68482.25

Authors

Huber, F.M.,Hoelz, A. (deposition date: 2016-10-23, release date: 2017-02-15, Last modification date: 2024-10-30)

Primary citation

Huber, F.M.,Hoelz, A.
Molecular basis for protection of ribosomal protein L4 from cellular degradation.
Nat Commun, 8:14354-14354, 2017

PubMed Abstract: Eukaryotic ribosome biogenesis requires the nuclear import of ∼80 nascent ribosomal proteins and the elimination of excess amounts by the cellular degradation machinery. Assembly chaperones recognize nascent unassembled ribosomal proteins and transport them together with karyopherins to their nuclear destination. We report the crystal structure of ribosomal protein L4 (RpL4) bound to its dedicated assembly chaperone of L4 (Acl4), revealing extensive interactions sequestering 70 exposed residues of the extended RpL4 loop. The observed molecular recognition fundamentally differs from canonical promiscuous chaperone-substrate interactions. We demonstrate that the eukaryote-specific RpL4 extension harbours overlapping binding sites for Acl4 and the nuclear transport factor Kap104, facilitating its continuous protection from the cellular degradation machinery. Thus, Acl4 serves a dual function to facilitate nuclear import and simultaneously protect unassembled RpL4 from the cellular degradation machinery.

PubMed: 28148929
DOI: 10.1038/ncomms14354

Experimental method

X-RAY DIFFRACTION (2.4 Å)