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1y42

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(New page: 200px<br /><applet load="1y42" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y42, resolution 1.95&Aring;" /> '''Crystal structure of...)
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[[Image:1y42.gif|left|200px]]<br /><applet load="1y42" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1y42, resolution 1.95&Aring;" />
caption="1y42, resolution 1.95&Aring;" />
'''Crystal structure of a C-terminally truncated CYT-18 protein'''<br />
'''Crystal structure of a C-terminally truncated CYT-18 protein'''<br />
==Overview==
==Overview==
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We determined a 1.95 A X-ray crystal structure of a C-terminally truncated, Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein), that functions in splicing group I introns. CYT-18's nucleotide binding, fold and intermediate alpha-helical domains superimpose on those of, bacterial TyrRSs, except for an N-terminal extension and two small, insertions not found in nonsplicing bacterial enzymes. These additions, surround the cyt-18-1 mutation site and are sites of suppressor mutations, that restore splicing, but not synthetase activity. Highly constrained, models based on directed hydroxyl radical cleavage assays show that the, group I intron binds at a site formed in part by the three additions on, the nucleotide binding fold surface opposite that which binds tRNATyr. Our, results show how essential proteins can progressively evolve new, functions.
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We determined a 1.95 A X-ray crystal structure of a C-terminally truncated Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) that functions in splicing group I introns. CYT-18's nucleotide binding fold and intermediate alpha-helical domains superimpose on those of bacterial TyrRSs, except for an N-terminal extension and two small insertions not found in nonsplicing bacterial enzymes. These additions surround the cyt-18-1 mutation site and are sites of suppressor mutations that restore splicing, but not synthetase activity. Highly constrained models based on directed hydroxyl radical cleavage assays show that the group I intron binds at a site formed in part by the three additions on the nucleotide binding fold surface opposite that which binds tRNATyr. Our results show how essential proteins can progressively evolve new functions.
==About this Structure==
==About this Structure==
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1Y42 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa] with TYR as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y42 OCA].
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1Y42 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa] with <scene name='pdbligand=TYR:'>TYR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y42 OCA].
==Reference==
==Reference==
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[[Category: Tyrosine--tRNA ligase]]
[[Category: Tyrosine--tRNA ligase]]
[[Category: Coon, R.]]
[[Category: Coon, R.]]
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[[Category: Lambowitz, A.M.]]
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[[Category: Lambowitz, A M.]]
[[Category: Madabusi, L.]]
[[Category: Madabusi, L.]]
[[Category: Monzingo, A.]]
[[Category: Monzingo, A.]]
[[Category: Nowakowski, J.]]
[[Category: Nowakowski, J.]]
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[[Category: Paukstelis, P.J.]]
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[[Category: Paukstelis, P J.]]
[[Category: Robertus, J.]]
[[Category: Robertus, J.]]
[[Category: TYR]]
[[Category: TYR]]
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[[Category: tyrosyl trna synthetase]]
[[Category: tyrosyl trna synthetase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:33:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:34 2008''

Revision as of 14:01, 21 February 2008


1y42, resolution 1.95Å

Drag the structure with the mouse to rotate

Crystal structure of a C-terminally truncated CYT-18 protein

Overview

We determined a 1.95 A X-ray crystal structure of a C-terminally truncated Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) that functions in splicing group I introns. CYT-18's nucleotide binding fold and intermediate alpha-helical domains superimpose on those of bacterial TyrRSs, except for an N-terminal extension and two small insertions not found in nonsplicing bacterial enzymes. These additions surround the cyt-18-1 mutation site and are sites of suppressor mutations that restore splicing, but not synthetase activity. Highly constrained models based on directed hydroxyl radical cleavage assays show that the group I intron binds at a site formed in part by the three additions on the nucleotide binding fold surface opposite that which binds tRNATyr. Our results show how essential proteins can progressively evolve new functions.

About this Structure

1Y42 is a Single protein structure of sequence from Neurospora crassa with as ligand. Active as Tyrosine--tRNA ligase, with EC number 6.1.1.1 Full crystallographic information is available from OCA.

Reference

A tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface., Paukstelis PJ, Coon R, Madabusi L, Nowakowski J, Monzingo A, Robertus J, Lambowitz AM, Mol Cell. 2005 Feb 4;17(3):417-28. PMID:15694342

Page seeded by OCA on Thu Feb 21 16:01:34 2008

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