5NT7

Structure of the LOTUS domain of Oskar in complex with the C-terminal RecA-like domain of Vasa

Summary for 5NT7

• Entry DOI: 10.2210/pdb5nt7/pdb
• Descriptor: ATP-dependent RNA helicase vasa, isoform A, Maternal effect protein oskar (3 entities in total)
• Functional Keywords: dead-box rna helicase, atpase, rna binding, regulator, stimulator, germ plasm, nuage, lotus, hydrolase- hydrolase regulator complex, hydrolase-hydrolase regulator complex, hydrolase/hydrolase regulator
• Biological source: Drosophila melanogaster (Fruit fly); More
• Cellular location: Cytoplasm : P09052
• Total number of polymer chains: 4
• Total formula weight: 60330.31

Authors

Jeske, M.,Ephrussi, A.,Mueller, C.W. (deposition date: 2017-04-27, release date: 2017-05-17, Last modification date: 2024-01-17)

Primary citation

Jeske, M.,Muller, C.W.,Ephrussi, A.
The LOTUS domain is a conserved DEAD-box RNA helicase regulator essential for the recruitment of Vasa to the germ plasm and nuage.
Genes Dev., 31:939-952, 2017

PubMed Abstract: DEAD-box RNA helicases play important roles in a wide range of metabolic processes. Regulatory proteins can stimulate or block the activity of DEAD-box helicases. Here, we show that LOTUS (Limkain, Oskar, and Tudor containing proteins 5 and 7) domains present in the germline proteins Oskar, TDRD5 (Tudor domain-containing 5), and TDRD7 bind and stimulate the germline-specific DEAD-box RNA helicase Vasa. Our crystal structure of the LOTUS domain of Oskar in complex with the C-terminal RecA-like domain of Vasa reveals that the LOTUS domain occupies a surface on a DEAD-box helicase not implicated previously in the regulation of the enzyme's activity. We show that, in vivo, the localization of Vasa to the nuage and germ plasm depends on its interaction with LOTUS domain proteins. The binding and stimulation of Vasa DEAD-box helicases by LOTUS domains are widely conserved.

PubMed: 28536148
DOI: 10.1101/gad.297051.117

Experimental method

X-RAY DIFFRACTION (1.4 Å)