Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase

Proceedings of the National Academy of Sciences of the United States of America - Tập 97 Số 24 - Trang 13080-13085 - 2000
J.M. Caruthers1, Eric R. Johnson1, David McKay1
1Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305

Tóm tắt

The eukaryotic translation initiation factor 4A (eIF4A) is a member of the DEA(D/H)-box RNA helicase family, a diverse group of proteins that couples an ATPase activity to RNA binding and unwinding. Previous work has provided the structure of the amino-terminal, ATP-binding domain of eIF4A. Extending those results, we have solved the structure of the carboxyl-terminal domain of eIF4A with data to 1.75 Å resolution; it has a parallel α-β topology that superimposes, with minor variations, on the structures and conserved motifs of the equivalent domain in other, distantly related helicases. Using data to 2.8 Å resolution and molecular replacement with the refined model of the carboxyl-terminal domain, we have completed the structure of full-length eIF4A; it is a “dumbbell” structure consisting of two compact domains connected by an extended linker. By using the structures of other helicases as a template, compact structures can be modeled for eIF4A that suggest ( i ) helicase motif IV binds RNA; ( ii ) Arg-298, which is conserved in the DEA(D/H)-box RNA helicase family but is absent from many other helicases, also binds RNA; and ( iii ) motifs V and VI “link” the carboxyl-terminal domain to the amino-terminal domain through interactions with ATP and the DEA(D/H) motif, providing a mechanism for coupling ATP binding and hydrolysis with conformational changes that modulate RNA binding.

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Thông tin xuất bản

Proceedings of the National Academy of Sciences of the United States of America

Tập 97 Số 24

13080-13085

Thông tin tác giả