1miw

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(New page: 200px<br /><applet load="1miw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1miw, resolution 3.00&Aring;" /> '''Crystal structure of...)
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[[Image:1miw.gif|left|200px]]<br /><applet load="1miw" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1miw.gif|left|200px]]<br /><applet load="1miw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1miw, resolution 3.00&Aring;" />
caption="1miw, resolution 3.00&Aring;" />
'''Crystal structure of Bacillus stearothermophilus CCA-adding enzyme in complex with ATP'''<br />
'''Crystal structure of Bacillus stearothermophilus CCA-adding enzyme in complex with ATP'''<br />
==Overview==
==Overview==
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CCA-adding enzymes polymerize CCA onto the 3' terminus of immature tRNAs, without using a nucleic acid template. The 3.0 A resolution crystal, structures of the CCA-adding enzyme from Bacillus stearothermophilus and, its complexes with ATP or CTP reveal a seahorse-shaped subunit consisting, of four domains: head, neck, body, and tail. The head is structurally, homologous to the palm domain of DNA polymerase beta but has additional, structural features and functions. The neck, body, and tail represent new, protein folding motifs. The neck provides a specific template for the, incoming ATP or CTP, whereas the body and tail may bind tRNA. Each subunit, has one active site capable of switching its base specificity between ATP, and CTP, an important component of the CCA-adding mechanism.
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CCA-adding enzymes polymerize CCA onto the 3' terminus of immature tRNAs without using a nucleic acid template. The 3.0 A resolution crystal structures of the CCA-adding enzyme from Bacillus stearothermophilus and its complexes with ATP or CTP reveal a seahorse-shaped subunit consisting of four domains: head, neck, body, and tail. The head is structurally homologous to the palm domain of DNA polymerase beta but has additional structural features and functions. The neck, body, and tail represent new protein folding motifs. The neck provides a specific template for the incoming ATP or CTP, whereas the body and tail may bind tRNA. Each subunit has one active site capable of switching its base specificity between ATP and CTP, an important component of the CCA-adding mechanism.
==About this Structure==
==About this Structure==
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1MIW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MIW OCA].
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1MIW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIW OCA].
==Reference==
==Reference==
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cho, H.D.]]
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[[Category: Cho, H D.]]
[[Category: Li, F.]]
[[Category: Li, F.]]
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[[Category: Steitz, T.A.]]
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[[Category: Steitz, T A.]]
[[Category: Wang, J.]]
[[Category: Wang, J.]]
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[[Category: Weiner, A.M.]]
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[[Category: Weiner, A M.]]
[[Category: Xiong, Y.]]
[[Category: Xiong, Y.]]
[[Category: ATP]]
[[Category: ATP]]
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[[Category: trna nucleotidyltransferase]]
[[Category: trna nucleotidyltransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:26:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:35 2008''

Revision as of 11:55, 21 February 2008


1miw, resolution 3.00Å

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Crystal structure of Bacillus stearothermophilus CCA-adding enzyme in complex with ATP

Overview

CCA-adding enzymes polymerize CCA onto the 3' terminus of immature tRNAs without using a nucleic acid template. The 3.0 A resolution crystal structures of the CCA-adding enzyme from Bacillus stearothermophilus and its complexes with ATP or CTP reveal a seahorse-shaped subunit consisting of four domains: head, neck, body, and tail. The head is structurally homologous to the palm domain of DNA polymerase beta but has additional structural features and functions. The neck, body, and tail represent new protein folding motifs. The neck provides a specific template for the incoming ATP or CTP, whereas the body and tail may bind tRNA. Each subunit has one active site capable of switching its base specificity between ATP and CTP, an important component of the CCA-adding mechanism.

About this Structure

1MIW is a Single protein structure of sequence from Geobacillus stearothermophilus with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP., Li F, Xiong Y, Wang J, Cho HD, Tomita K, Weiner AM, Steitz TA, Cell. 2002 Dec 13;111(6):815-24. PMID:12526808

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