1px5

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(New page: 200px<br /><applet load="1px5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1px5, resolution 1.74&Aring;" /> '''Crystal structure of...)
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[[Image:1px5.gif|left|200px]]<br /><applet load="1px5" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1px5.gif|left|200px]]<br /><applet load="1px5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1px5, resolution 1.74&Aring;" />
caption="1px5, resolution 1.74&Aring;" />
'''Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase'''<br />
'''Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase'''<br />
==Overview==
==Overview==
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2'-5'-oligoadenylate synthetases are interferon-induced, double-stranded, RNA-activated antiviral enzymes which are the only proteins known to, catalyze 2'-specific nucleotidyl transfer. This crystal structure of a, 2'-5'-oligoadenylate synthetase reveals a structural conservation with the, 3'-specific poly(A) polymerase that, coupled with structure-guided, mutagenesis, supports a conserved catalytic mechanism for the 2'- and, 3'-specific nucleotidyl transferases. Comparison with structures of other, superfamily members indicates that the donor substrates are bound by, conserved active site features while the acceptor substrates are oriented, by nonconserved regions. The 2'-5'-oligoadenylate synthetases are, activated by viral double-stranded RNA in infected cells and initiate a, cellular response by synthesizing 2'-5'-oligoadenylates, which in turn, activate RNase L. This crystal structure suggests that activation involves, a domain-domain shift and identifies a putative dsRNA activation site that, is probed by mutagenesis, thus providing structural insight into cellular, recognition of viral double-stranded RNA.
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2'-5'-oligoadenylate synthetases are interferon-induced, double-stranded RNA-activated antiviral enzymes which are the only proteins known to catalyze 2'-specific nucleotidyl transfer. This crystal structure of a 2'-5'-oligoadenylate synthetase reveals a structural conservation with the 3'-specific poly(A) polymerase that, coupled with structure-guided mutagenesis, supports a conserved catalytic mechanism for the 2'- and 3'-specific nucleotidyl transferases. Comparison with structures of other superfamily members indicates that the donor substrates are bound by conserved active site features while the acceptor substrates are oriented by nonconserved regions. The 2'-5'-oligoadenylate synthetases are activated by viral double-stranded RNA in infected cells and initiate a cellular response by synthesizing 2'-5'-oligoadenylates, which in turn activate RNase L. This crystal structure suggests that activation involves a domain-domain shift and identifies a putative dsRNA activation site that is probed by mutagenesis, thus providing structural insight into cellular recognition of viral double-stranded RNA.
==About this Structure==
==About this Structure==
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1PX5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PX5 OCA].
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1PX5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PX5 OCA].
==Reference==
==Reference==
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[[Category: Hartmann, R.]]
[[Category: Hartmann, R.]]
[[Category: Justesen, J.]]
[[Category: Justesen, J.]]
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[[Category: Sarkar, S.N.]]
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[[Category: Sarkar, S N.]]
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[[Category: Sen, G.C.]]
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[[Category: Sen, G C.]]
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[[Category: Yee, V.C.]]
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[[Category: Yee, V C.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: 5-stranded antiparalel beta sheet]]
[[Category: 5-stranded antiparalel beta sheet]]
[[Category: four helix bundle]]
[[Category: four helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:12:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:30 2008''

Revision as of 12:33, 21 February 2008


1px5, resolution 1.74Å

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Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase

Overview

2'-5'-oligoadenylate synthetases are interferon-induced, double-stranded RNA-activated antiviral enzymes which are the only proteins known to catalyze 2'-specific nucleotidyl transfer. This crystal structure of a 2'-5'-oligoadenylate synthetase reveals a structural conservation with the 3'-specific poly(A) polymerase that, coupled with structure-guided mutagenesis, supports a conserved catalytic mechanism for the 2'- and 3'-specific nucleotidyl transferases. Comparison with structures of other superfamily members indicates that the donor substrates are bound by conserved active site features while the acceptor substrates are oriented by nonconserved regions. The 2'-5'-oligoadenylate synthetases are activated by viral double-stranded RNA in infected cells and initiate a cellular response by synthesizing 2'-5'-oligoadenylates, which in turn activate RNase L. This crystal structure suggests that activation involves a domain-domain shift and identifies a putative dsRNA activation site that is probed by mutagenesis, thus providing structural insight into cellular recognition of viral double-stranded RNA.

About this Structure

1PX5 is a Single protein structure of sequence from Sus scrofa with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase., Hartmann R, Justesen J, Sarkar SN, Sen GC, Yee VC, Mol Cell. 2003 Nov;12(5):1173-85. PMID:14636576

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