PDBsum entry 5lhx

Structural protein

PDB id: 5lhx

Contents

Protein chains

87 a.a.

Waters ×35

PDB id:

5lhx

Name:

Structural protein

Title:

Pb3 domain of drosophila melanogaster plk4 (sak)

Structure:

Serine/threonine-protein kinase plk4. Chain: a, b. Fragment: unp residues 657-745. Synonym: polo-like kinase 4,plk-4,serine/threonine-protein kinase sak. Engineered: yes

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: sak, cg7186. Expressed in: escherichia coli b. Expression_system_taxid: 37762.

Resolution:

1.53Å R-factor: 0.169 R-free: 0.209

Authors:

M.A.Cottee,S.M.Lea

Key ref:

M.A.Cottee et al. (2017). A key centriole assembly interaction interface between human PLK4 and STIL appears to not be conserved in flies. Biol Open, 6, 381-389. PubMed id: 28202467 DOI: 10.1242/bio.024661

Date:

13-Jul-16 Release date: 01-Mar-17

Protein chains

O97143  (PLK4_DROME) -  Serine/threonine-protein kinase PLK4 from Drosophila melanogaster

Seq: 769 a.a.

Struc: 87 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.21 - polo kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

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

reference

DOI no: 10.1242/bio.024661

Biol Open 6:381-389 (2017)

PubMed id: 28202467

A key centriole assembly interaction interface between human PLK4 and STIL appears to not be conserved in flies.

M.A.Cottee, S.Johnson, J.W.Raff, S.M.Lea.

ABSTRACT

A small number of proteins form a conserved pathway of centriole duplication. In humans and flies, the binding of PLK4/Sak to STIL/Ana2 initiates daughter centriole assembly. In humans, this interaction is mediated by an interaction between the Polo-Box-3 (PB3) domain of PLK4 and the coiled-coil domain of STIL (HsCCD). We showed previously that the Drosophila Ana2 coiled-coil domain (DmCCD) is essential for centriole assembly, but it forms a tight parallel tetramer in vitro that likely precludes an interaction with PB3. Here, we show that the isolated HsCCD and HsPB3 domains form a mixture of homo-multimers in vitro, but these readily dissociate when mixed to form the previously described 1:1 HsCCD:HsPB3 complex. In contrast, although Drosophila PB3 (DmPB3) adopts a canonical polo-box fold, it does not detectably interact with DmCCD in vitro Thus, surprisingly, a key centriole assembly interaction interface appears to differ between humans and flies.