1fuu
From Proteopedia
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YEAST INITIATION FACTOR 4A
Overview
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.
About this Structure
1FUU is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase., Caruthers JM, Johnson ER, McKay DB, Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13080-5. PMID:11087862
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