1fuk: Difference between revisions

Revision as of 03:58, 1 July 2008

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File:1fuk.png

Template:STRUCTURE 1fuk

CRYSTAL STRUCTURE OF THE CARBOXY TERMINAL DOMAIN OF YEAST EIF4ACRYSTAL STRUCTURE OF THE CARBOXY TERMINAL DOMAIN OF YEAST EIF4A

Template:ABSTRACT PUBMED 11087862

About this StructureAbout this Structure

1FUK is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

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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 {{STRUCTURE_1fuk|  PDB=1fuk  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE CARBOXY TERMINAL DOMAIN OF YEAST EIF4A'''
+===CRYSTAL STRUCTURE OF THE CARBOXY TERMINAL DOMAIN OF YEAST EIF4A===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11087862}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11087862 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11087862}}
 ==About this Structure==
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 [[Category: Helicase]]
 [[Category: Initiation factor 4a]]
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