PDBsum entry 5by8

Biosynthetic protein

PDB id: 5by8

Contents

Protein chains

241 a.a.

85 a.a.

Waters ×425

PDB id:

5by8

Name:

Biosynthetic protein

Title:

The structure of rpf2-rrs1 explains its role in ribosome biogenesis

Structure:

Rpf2. Chain: a. Engineered: yes. Rrs1. Chain: b. Engineered: yes

Source:

Emericella nidulans fgsc a4. Organism_taxid: 227321. Gene: ania_10200. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: an3745.2, ania_03745. Expression_system_taxid: 562

Resolution:

1.52Å R-factor: 0.148 R-free: 0.191

Authors:

S.Kharde,F.R.Calvino,A.Gumiero,K.Wild,I.Sinning

Key ref:

S.Kharde et al. (2015). The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis. Nucleic Acids Res, 43, 7083-7095. PubMed id: 26117542 DOI: 10.1093/nar/gkv640

Date:

10-Jun-15 Release date: 08-Jul-15

Protein chain

C8VMF9  (C8VMF9_EMENI) -  Ribosome production factor 2 homolog from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)

Seq: 331 a.a.

Struc: 241 a.a.*

Protein chain

Q5B6T5  (Q5B6T5_EMENI) -  Ribosome biogenesis regulatory protein from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)

Seq: 218 a.a.

Struc: 85 a.a.

* PDB and UniProt seqs differ at 10 residue positions (black crosses)

DOI no: 10.1093/nar/gkv640

Nucleic Acids Res 43:7083-7095 (2015)

PubMed id: 26117542

The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis.

S.Kharde, F.R.Calviño, A.Gumiero, K.Wild, I.Sinning.

ABSTRACT

The assembly of eukaryotic ribosomes is a hierarchical process involving about 200 biogenesis factors and a series of remodeling steps. The 5S RNP consisting of the 5S rRNA, RpL5 and RpL11 is recruited at an early stage, but has to rearrange during maturation of the pre-60S ribosomal subunit. Rpf2 and Rrs1 have been implicated in 5S RNP biogenesis, but their precise role was unclear. Here, we present the crystal structure of the Rpf2-Rrs1 complex from Aspergillus nidulans at 1.5 Å resolution and describe it as Brix domain of Rpf2 completed by Rrs1 to form two anticodon-binding domains with functionally important tails. Fitting the X-ray structure into the cryo-EM density of a previously described pre-60S particle correlates with biochemical data. The heterodimer forms specific contacts with the 5S rRNA, RpL5 and the biogenesis factor Rsa4. The flexible protein tails of Rpf2-Rrs1 localize to the central protuberance. Two helices in the Rrs1 C-terminal tail occupy a strategic position to block the rotation of 25S rRNA and the 5S RNP. Our data provide a structural model for 5S RNP recruitment to the pre-60S particle and explain why removal of Rpf2-Rrs1 is necessary for rearrangements to drive 60S maturation.