PDBsum entry 4buj

Hydrolase

PDB id: 4buj

Contents

Protein chains

903 a.a.

1367 a.a.

392 a.a.

351 a.a.

Ligands

SO4 ×20

PDB id:

4buj

Name:

Hydrolase

Title:

Crystal structure of the s. Cerevisiae ski2-3-8 complex

Structure:

Antiviral helicase ski2. Chain: a, e. Fragment: residues 1-834,1086-1287. Synonym: superkiller protein 2, ski2. Engineered: yes. Other_details: residues 835-1085 replaced by a gly-ser-arg-gly linker. Superkiller protein 3. Chain: b, f.

Source:

Saccharomyces cerevisiae. Organism_taxid: 559292. Strain: s288c. Expressed in: trichoplusia ni. Expression_system_taxid: 7111.

Resolution:

3.70Å R-factor: 0.233 R-free: 0.265

Authors:

F.Halbach,P.Reichelt,M.Rode,E.Conti

Key ref:

F.Halbach et al. (2013). The yeast ski complex: crystal structure and RNA channeling to the exosome complex. Cell, 154, 814-826. PubMed id: 23953113 DOI: 10.1016/j.cell.2013.07.017

Date:

20-Jun-13 Release date: 28-Aug-13

Protein chains

P35207  (SKI2_YEAST) -  Antiviral helicase SKI2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1287 a.a.

Struc: 903 a.a.*

Protein chains

P17883  (SKI3_YEAST) -  Superkiller protein 3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1432 a.a.

Struc: 1367 a.a.

Protein chains

Q02793  (SKI8_YEAST) -  Antiviral protein SKI8 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 397 a.a.

Struc: 392 a.a.

Protein chain

Q02793  (SKI8_YEAST) -  Antiviral protein SKI8 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 397 a.a.

Struc: 351 a.a.

* PDB and UniProt seqs differ at 53 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, E: E.C.3.6.4.13 - Rna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.cell.2013.07.017

Cell 154:814-826 (2013)

PubMed id: 23953113

The yeast ski complex: crystal structure and RNA channeling to the exosome complex.

F.Halbach, P.Reichelt, M.Rode, E.Conti.

ABSTRACT

The Ski complex is a conserved multiprotein assembly required for the cytoplasmic functions of the exosome, including RNA turnover, surveillance, and interference. Ski2, Ski3, and Ski8 assemble in a tetramer with 1:1:2 stoichiometry. The crystal structure of an S. cerevisiae 370 kDa core complex shows that Ski3 forms an array of 33 TPR motifs organized in N-terminal and C-terminal arms. The C-terminal arm of Ski3 and the two Ski8 subunits position the helicase core of Ski2 centrally within the complex, enhancing RNA binding. The Ski3 N-terminal arm and the Ski2 insertion domain allosterically modulate the ATPase and helicase activities of the complex. Biochemical data suggest that the Ski complex can thread RNAs directly to the exosome, coupling the helicase and the exoribonuclease through a continuous RNA channel. Finally, we identify a Ski8-binding motif common to Ski3 and Spo11, rationalizing the moonlighting properties of Ski8 in mRNA decay and meiosis.