7DTJ

Crystal structure of the RecA2 domain of RNA helicase CGH-1 in C. elegans

Summary for 7DTJ

• Entry DOI: 10.2210/pdb7dtj/pdb
• Descriptor: ATP-dependent RNA helicase cgh-1 (2 entities in total)
• Functional Keywords: helicase, rna binding, rna binding protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 1
• Total formula weight: 21488.69

Authors

Zhang, Y.,Lv, M.Q.,Hong, J.J. (deposition date: 2021-01-05, release date: 2021-03-17, Last modification date: 2023-11-29)

Primary citation

Zhang, Y.,Lv, M.,Li, F.,Li, M.,Zhang, J.,Shi, Y.,Hong, J.
Structural and biochemical insights into the recognition of RNA helicase CGH-1 by CAR-1 in C. elegans.
Biochem.Biophys.Res.Commun., 549:135-142, 2021

PubMed Abstract: A protein-RNA complex containing the RNA helicase CGH-1 and a germline specific RNA-binding protein CAR-1 is involved in various aspects of function in C. elegans. However, the structural basis for the assembly of this protein complex remains unclear. Here, we elucidate the molecular basis of the recognition of CGH-1 by CAR-1. Additionally, we found that the ATPase activity of CGH-1 is stimulated by NTL-1a MIF4G domain in vitro. Furthermore, we determined the structures of the two RecA-like domains of CGH-1 by X-ray crystallography at resolutions of 1.85 and 2.40 Å, respectively. Structural and biochemical approaches revealed a bipartite interface between CGH-1 RecA2 and the FDF-TFG motif of CAR-1. NMR and structure-based mutations in CGH-1 RecA2 or CAR-1 attenuated or disrupted CGH-1 binding to CAR-1, assessed by ITC and GST-pulldown in vitro. These findings provide insights into a conserved mechanism in the recognition of CGH-1 by CAR-1. Together, our data provide the missing physical links in understanding the assembly and function of CGH-1 and CAR-1 in C. elegans.

PubMed: 33676181
DOI: 10.1016/j.bbrc.2021.02.119

Experimental method

X-RAY DIFFRACTION (2.402 Å)