5AL7

N-terminal fragment of Drosophila melanogaster Sas-6 (F143D), dimerised via the coiled-coil domain.

Summary for 5AL7

• Entry DOI: 10.2210/pdb5al7/pdb
• Related: 5AL6
• Descriptor: SPINDLE ASSEMBLY ABNORMAL PROTEIN 6 HOMOLOG, NITRATE ION (3 entities in total)
• Functional Keywords: structural protein, centriole, cartwheel
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY)
• Total number of polymer chains: 2
• Total formula weight: 50460.92

Authors

Cottee, M.A.,Johnson, S.,Lea, S.M. (deposition date: 2015-03-06, release date: 2015-06-03, Last modification date: 2024-01-10)

Primary citation

Cottee, M.A.,Muschalik, N.,Johnson, S.,Leveson, J.,Raff, J.W.,Lea, S.M.
The homo-oligomerisation of both Sas-6 and Ana2 is required for efficient centriole assembly in flies.
Elife, 4:e07236-e07236, 2015

PubMed Abstract: Sas-6 and Ana2/STIL proteins are required for centriole duplication and the homo-oligomerisation properties of Sas-6 help establish the ninefold symmetry of the central cartwheel that initiates centriole assembly. Ana2/STIL proteins are poorly conserved, but they all contain a predicted Central Coiled-Coil Domain (CCCD). Here we show that the Drosophila Ana2 CCCD forms a tetramer, and we solve its structure to 0.8 Å, revealing that it adopts an unusual parallel-coil topology. We also solve the structure of the Drosophila Sas-6 N-terminal domain to 2.9 Å revealing that it forms higher-order oligomers through canonical interactions. Point mutations that perturb Sas-6 or Ana2 homo-oligomerisation in vitro strongly perturb centriole assembly in vivo. Thus, efficient centriole duplication in flies requires the homo-oligomerisation of both Sas-6 and Ana2, and the Ana2 CCCD tetramer structure provides important information on how these proteins might cooperate to form a cartwheel structure.

PubMed: 26002084
DOI: 10.7554/eLife.07236

Experimental method

X-RAY DIFFRACTION (2.92 Å)