1fuk: Difference between revisions

New page: left|200px<br /><applet load="1fuk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fuk, resolution 1.75Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1fuk.jpg|left|200px]]<br /><applet load="1fuk" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1fuk.jpg|left|200px]]<br /><applet load="1fuk" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fuk, resolution 1.75&Aring;" />
caption="1fuk, resolution 1.75&Aring;" />
'''CRYSTAL STRUCTURE OF THE CARBOXY TERMINAL DOMAIN OF YEAST EIF4A'''<br />
'''CRYSTAL STRUCTURE OF THE CARBOXY TERMINAL DOMAIN OF YEAST EIF4A'''<br />


==Overview==
==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 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==
==About this Structure==
1FUK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FUK OCA].  
1FUK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUK OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Caruthers, J.M.]]
[[Category: Caruthers, J M.]]
[[Category: Johnson, E.R.]]
[[Category: Johnson, E R.]]
[[Category: McKay, D.B.]]
[[Category: McKay, D B.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: dead-box protein]]
[[Category: dead-box protein]]
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[[Category: initiation factor 4a]]
[[Category: initiation factor 4a]]


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