1FUU

YEAST INITIATION FACTOR 4A

Summary for 1FUU

• Entry DOI: 10.2210/pdb1fuu/pdb
• Descriptor: YEAST INITIATION FACTOR 4A (2 entities in total)
• Functional Keywords: if4a, helicase, dead-box protein, translation
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P10081
• Total number of polymer chains: 2
• Total formula weight: 90261.27

Authors

Caruthers, J.M.,Johnson, E.R.,McKay, D.B. (deposition date: 2000-09-15, release date: 2000-11-29, Last modification date: 2024-11-20)

Primary citation

Caruthers, J.M.,Johnson, E.R.,McKay, D.B.
Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase.
Proc.Natl.Acad.Sci.USA, 97:13080-13085, 2000

PubMed Abstract: 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 A resolution; it has a parallel alpha-beta 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 A 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.

PubMed: 11087862
DOI: 10.1073/pnas.97.24.13080

Experimental method

X-RAY DIFFRACTION (2.5 Å)