1qva

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(New page: 200px<br /><applet load="1qva" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qva, resolution 2.50&Aring;" /> '''YEAST INITIATION FAC...)
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'''YEAST INITIATION FACTOR 4A N-TERMINAL DOMAIN'''<br />
'''YEAST INITIATION FACTOR 4A N-TERMINAL DOMAIN'''<br />
==Overview==
==Overview==
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The eukaryotic translation initiation factor 4A (elF4A) is a, representative of the DEAD-box RNA helicase protein family. We have solved, the crystallographic structure of the amino-terminal domain (residues, 1-223) of yeast elF4A. The domain is built around a core scaffold, a, parallel alpha-beta motif with five beta strands, that is found in other, RNA and DNA helicases, as well as in the RecA protein. The amino acid, sequence motifs that are conserved within the helicase family are, localized to the beta strand--&gt;alpha helix junctions within the core. The, core of the amino terminal domain of elF4A is amplified with additional, structural elements that differ from those of other helicases. The, phosphate binding loop (the Walker A motif) is in an unusual closed, conformation. The crystallographic structure reveals specific interactions, between amino acid residues of the phosphate binding loop, the DEAD motif, and the SAT motif, whose alteration is known to impair coupling between, the ATPase cycle and the RNA unwinding activity of elF4A.
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The eukaryotic translation initiation factor 4A (elF4A) is a representative of the DEAD-box RNA helicase protein family. We have solved the crystallographic structure of the amino-terminal domain (residues 1-223) of yeast elF4A. The domain is built around a core scaffold, a parallel alpha-beta motif with five beta strands, that is found in other RNA and DNA helicases, as well as in the RecA protein. The amino acid sequence motifs that are conserved within the helicase family are localized to the beta strand--&gt;alpha helix junctions within the core. The core of the amino terminal domain of elF4A is amplified with additional structural elements that differ from those of other helicases. The phosphate binding loop (the Walker A motif) is in an unusual closed conformation. The crystallographic structure reveals specific interactions between amino acid residues of the phosphate binding loop, the DEAD motif, and the SAT motif, whose alteration is known to impair coupling between the ATPase cycle and the RNA unwinding activity of elF4A.
==About this Structure==
==About this Structure==
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1QVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QVA OCA].
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1QVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVA OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Johnson, E.R.]]
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[[Category: Johnson, E R.]]
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[[Category: McKay, D.B.]]
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[[Category: McKay, D B.]]
[[Category: dead box]]
[[Category: dead box]]
[[Category: eif4a]]
[[Category: eif4a]]
[[Category: rna helicase]]
[[Category: rna helicase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:01:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:03 2008''

Revision as of 12:44, 21 February 2008


1qva, resolution 2.50Å

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YEAST INITIATION FACTOR 4A N-TERMINAL DOMAIN

Overview

The eukaryotic translation initiation factor 4A (elF4A) is a representative of the DEAD-box RNA helicase protein family. We have solved the crystallographic structure of the amino-terminal domain (residues 1-223) of yeast elF4A. The domain is built around a core scaffold, a parallel alpha-beta motif with five beta strands, that is found in other RNA and DNA helicases, as well as in the RecA protein. The amino acid sequence motifs that are conserved within the helicase family are localized to the beta strand-->alpha helix junctions within the core. The core of the amino terminal domain of elF4A is amplified with additional structural elements that differ from those of other helicases. The phosphate binding loop (the Walker A motif) is in an unusual closed conformation. The crystallographic structure reveals specific interactions between amino acid residues of the phosphate binding loop, the DEAD motif, and the SAT motif, whose alteration is known to impair coupling between the ATPase cycle and the RNA unwinding activity of elF4A.

About this Structure

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

Reference

Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase., Johnson ER, McKay DB, RNA. 1999 Dec;5(12):1526-34. PMID:10606264

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