PDBsum entry 4uzz

Motor protein

PDB id: 4uzz

Contents

Protein chains

108 a.a.

65 a.a.

Waters ×3

PDB id:

4uzz

Name:

Motor protein

Title:

Crystal structure of the ttift52-46 complex

Structure:

Intraflagellar transport complex b protein 46 carboxy- terminal protein. Chain: a. Fragment: c-terminal domain, residues 221-332. Synonym: intraflagellar transport protein 46. Engineered: yes. Intraflagellar transporter-like protein. Chain: b. Fragment: c-terminal domain, residues 371-434.

Source:

Tetrahymena thermophila. Organism_taxid: 5911. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.32Å R-factor: 0.241 R-free: 0.264

Authors:

P.Braeuer,M.Taschner,E.Lorentzen

Key ref:

M.Taschner et al. (2014). Crystal structures of IFT70/52 and IFT52/46 provide insight into intraflagellar transport B core complex assembly. J Cell Biol, 207, 269-282. PubMed id: 25349261 DOI: 10.1083/jcb.201408002

Date:

09-Sep-14 Release date: 05-Nov-14

Protein chain

Q23KH7  (Q23KH7_TETTS) -  Intraflagellar transport complex B protein 46 carboxy-terminal protein from Tetrahymena thermophila (strain SB210)

Seq: 342 a.a.

Struc: 108 a.a.*

Protein chain

I7LT74  (I7LT74_TETTS) -  Intraflagellar transporter-like protein from Tetrahymena thermophila (strain SB210)

Seq: 434 a.a.

Struc: 65 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1083/jcb.201408002

J Cell Biol 207:269-282 (2014)

PubMed id: 25349261

Crystal structures of IFT70/52 and IFT52/46 provide insight into intraflagellar transport B core complex assembly.

M.Taschner, F.Kotsis, P.Braeuer, E.W.Kuehn, E.Lorentzen.

ABSTRACT

Cilia are microtubule-based organelles that assemble via intraflagellar transport (IFT) and function as signaling hubs on eukaryotic cells. IFT relies on molecular motors and IFT complexes that mediate the contacts with ciliary cargo. To elucidate the architecture of the IFT-B complex, we reconstituted and purified the nonameric IFT-B core from Chlamydomonas reinhardtii and determined the crystal structures of C. reinhardtii IFT70/52 and Tetrahymena IFT52/46 subcomplexes. The 2.5-Å resolution IFT70/52 structure shows that IFT52330-370 is buried deeply within the IFT70 tetratricopeptide repeat superhelix. Furthermore, the polycystic kidney disease protein IFT88 binds IFT52281-329 in a complex that interacts directly with IFT70/IFT52330-381 in trans. The structure of IFT52C/IFT46C was solved at 2.3 Å resolution, and we show that it is essential for IFT-B core integrity by mediating interaction between IFT88/70/52/46 and IFT81/74/27/25/22 subcomplexes. Consistent with this, overexpression of mammalian IFT52C in MDCK cells is dominant-negative and causes IFT protein mislocalization and disrupted ciliogenesis. These data further rationalize several ciliogenesis phenotypes of IFT mutant strains.