PDBsum entry 5yv5

Translation

PDB id: 5yv5

Contents

Protein chains

517 a.a.

14 a.a.

Ligands

ADP ×2

Metals

_MG ×2

Waters ×292

PDB id:

5yv5

Name:

Translation

Title:

Crystal structure of the complex of archaeal ribosomal stalk protein ap1 and archaeal ribosome recycling factor aabce1.

Structure:

Atpase ril. Chain: a. Engineered: yes. Archaeal ribosomal stalk protein ap1. Chain: b. Engineered: yes

Source:

Pyrococcus furiosus com1. Organism_taxid: 1185654. Gene: pfc_02505. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Pyrococcus furiosus. Organism_taxid: 2261

Resolution:

2.10Å R-factor: 0.197 R-free: 0.244

Authors:

H.Imai,T.Abe,T.Miyoshi,S.Nishikawa,K.Ito,T.Uchiumi

Key ref:

H.Imai et al. (2018). The ribosomal stalk protein is crucial for the action of the conserved ATPase ABCE1. Nucleic Acids Res, 46, 7820-7830. PubMed id: 30010948

Date:

24-Nov-17 Release date: 18-Jul-18

Protein chain

I6V0C7  (I6V0C7_9EURY) -  ATPase RIL from Pyrococcus furiosus COM1

Seq: 590 a.a.

Struc: 517 a.a.*

Protein chain

Q8TZJ7  (Q8TZJ7_PYRFU) -  Large ribosomal subunit protein P1 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Seq: 107 a.a.

Struc: 14 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Nucleic Acids Res 46:7820-7830 (2018)

PubMed id: 30010948

The ribosomal stalk protein is crucial for the action of the conserved ATPase ABCE1.

H.Imai, T.Abe, T.Miyoshi, S.I.Nishikawa, K.Ito, T.Uchiumi.

ABSTRACT

The ATP-binding cassette (ABC) protein ABCE1 is an essential factor in ribosome recycling during translation. However, the detailed mechanochemistry of its recruitment to the ribosome, ATPase activation and subunit dissociation remain to be elucidated. Here, we show that the ribosomal stalk protein, which is known to participate in the actions of translational GTPase factors, plays an important role in these events. Biochemical and crystal structural data indicate that the conserved hydrophobic amino acid residues at the C-terminus of the archaeal stalk protein aP1 binds to the nucleotide-binding domain 1 (NBD1) of aABCE1, and that this binding is crucial for ATPase activation of aABCE1 on the ribosome. The functional role of the stalk•ABCE1 interaction in ATPase activation and the subunit dissociation is also investigated using mutagenesis in a yeast system. The data demonstrate that the ribosomal stalk protein likely participates in efficient actions of both archaeal and eukaryotic ABCE1 in ribosome recycling. The results also show that the stalk protein has a role in the function of ATPase as well as GTPase factors in translation.