Long-range conformational changes in the nucleotide-bound states of the DEAD-box helicase Vasa.

ABSTRACT: DEAD-box helicases use ATP to unwind short double-stranded RNA (dsRNA). The helicase core consists of two discrete domains, termed RecA_N and RecA_C. The nucleotide binding site is harbored in RecA_N, while both RecA_N and RecA_C are involved in RNA recognition and ATP hydrolysis. In the absence of nucleotides or RNA, RecA_N and RecA_C do not interact ("open" form of the enzyme). In the presence of both RNA and ATP the two domains come together ("closed" form), building the composite RNA binding site and stimulating ATP hydrolysis. Because of the different roles and thermodynamic properties of the ADP-bound and ATP-bound states in the catalytic cycle, the conformations of DEAD-box helicases in complex with ATP and ADP are assumed to be different. However, the available crystal structures d

SUBMITTER: Codutti L 

PROVIDER: S-EPMC11617632 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature