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1lj2

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(New page: 200px<br /> <applet load="1lj2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lj2, resolution 2.38&Aring;" /> '''Recognition of eIF4...)
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[[Image:1lj2.gif|left|200px]]<br />
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[[Image:1lj2.gif|left|200px]]<br /><applet load="1lj2" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1lj2" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1lj2, resolution 2.38&Aring;" />
caption="1lj2, resolution 2.38&Aring;" />
'''Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization'''<br />
'''Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization'''<br />
==Overview==
==Overview==
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Rotaviruses, segmented double-stranded RNA viruses, co-opt the eukaryotic, translation machinery with the aid of nonstructural protein 3 (NSP3), a, rotaviral functional homolog of the cellular poly(A) binding protein, (PABP). NSP3 binds to viral mRNA 3' consensus sequences and circularizes, mRNA via interactions with eIF4G. Here, we present the X-ray structure of, the C-terminal domain of NSP3 (NSP3-C) recognizing a fragment of eIF4GI., Homodimerization of NSP3-C yields a symmetric, elongated, largely, alpha-helical structure with two hydrophobic eIF4G binding pockets at the, dimer interface. Site-directed mutagenesis and isothermal titration, calorimetry documented that NSP3 and PABP use analogous eIF4G recognition, strategies, despite marked differences in tertiary structure.
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Rotaviruses, segmented double-stranded RNA viruses, co-opt the eukaryotic translation machinery with the aid of nonstructural protein 3 (NSP3), a rotaviral functional homolog of the cellular poly(A) binding protein (PABP). NSP3 binds to viral mRNA 3' consensus sequences and circularizes mRNA via interactions with eIF4G. Here, we present the X-ray structure of the C-terminal domain of NSP3 (NSP3-C) recognizing a fragment of eIF4GI. Homodimerization of NSP3-C yields a symmetric, elongated, largely alpha-helical structure with two hydrophobic eIF4G binding pockets at the dimer interface. Site-directed mutagenesis and isothermal titration calorimetry documented that NSP3 and PABP use analogous eIF4G recognition strategies, despite marked differences in tertiary structure.
==About this Structure==
==About this Structure==
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1LJ2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Simian_rotavirus_a/sa11 Simian rotavirus a/sa11] with AU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LJ2 OCA].
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1LJ2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Simian_rotavirus_a/sa11 Simian rotavirus a/sa11] with <scene name='pdbligand=AU:'>AU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJ2 OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Simian rotavirus a/sa11]]
[[Category: Simian rotavirus a/sa11]]
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[[Category: Burley, S.K.]]
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[[Category: Burley, S K.]]
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[[Category: Groft, C.M.]]
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[[Category: Groft, C M.]]
[[Category: AU]]
[[Category: AU]]
[[Category: nsp3; homodimer; eif4g; rotavirus; translation; mrna; closed loop; coiled coil]]
[[Category: nsp3; homodimer; eif4g; rotavirus; translation; mrna; closed loop; coiled coil]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:01:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:22 2008''

Revision as of 11:45, 21 February 2008


1lj2, resolution 2.38Å

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Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization

Overview

Rotaviruses, segmented double-stranded RNA viruses, co-opt the eukaryotic translation machinery with the aid of nonstructural protein 3 (NSP3), a rotaviral functional homolog of the cellular poly(A) binding protein (PABP). NSP3 binds to viral mRNA 3' consensus sequences and circularizes mRNA via interactions with eIF4G. Here, we present the X-ray structure of the C-terminal domain of NSP3 (NSP3-C) recognizing a fragment of eIF4GI. Homodimerization of NSP3-C yields a symmetric, elongated, largely alpha-helical structure with two hydrophobic eIF4G binding pockets at the dimer interface. Site-directed mutagenesis and isothermal titration calorimetry documented that NSP3 and PABP use analogous eIF4G recognition strategies, despite marked differences in tertiary structure.

About this Structure

1LJ2 is a Protein complex structure of sequences from Simian rotavirus a/sa11 with as ligand. Full crystallographic information is available from OCA.

Reference

Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization., Groft CM, Burley SK, Mol Cell. 2002 Jun;9(6):1273-83. PMID:12086624

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