1gid

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(New page: 200px<br /><applet load="1gid" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gid, resolution 2.500&Aring;" /> '''CRYSTAL STRUCTURE O...)
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'''CRYSTAL STRUCTURE OF A GROUP I RIBOZYME DOMAIN: PRINCIPLES OF RNA PACKING'''<br />
'''CRYSTAL STRUCTURE OF A GROUP I RIBOZYME DOMAIN: PRINCIPLES OF RNA PACKING'''<br />
==Overview==
==Overview==
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Group I self-splicing introns catalyze their own excision from precursor, RNAs by way of a two-step transesterification reaction. The catalytic core, of these ribozymes is formed by two structural domains. The 2.8-angstrom, crystal structure of one of these, the P4-P6 domain of the Tetrahymena, thermophila intron, is described. In the 160-nucleotide domain, a sharp, bend allows stacked helices of the conserved core to pack alongside, helices of an adjacent region. Two specific long-range interactions clamp, the two halves of the domain together: a two-Mg2+-coordinated, adenosine-rich corkscrew plugs into the minor groove of a helix, and a, GAAA hairpin loop binds to a conserved 11-nucleotide internal loop. Metal-, and ribose-mediated backbone contacts further stabilize the close, side-by-side helical packing. The structure indicates the extent of RNA, packing required for the function of large ribozymes, the spliceosome, and, the ribosome.
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Group I self-splicing introns catalyze their own excision from precursor RNAs by way of a two-step transesterification reaction. The catalytic core of these ribozymes is formed by two structural domains. The 2.8-angstrom crystal structure of one of these, the P4-P6 domain of the Tetrahymena thermophila intron, is described. In the 160-nucleotide domain, a sharp bend allows stacked helices of the conserved core to pack alongside helices of an adjacent region. Two specific long-range interactions clamp the two halves of the domain together: a two-Mg2+-coordinated adenosine-rich corkscrew plugs into the minor groove of a helix, and a GAAA hairpin loop binds to a conserved 11-nucleotide internal loop. Metal- and ribose-mediated backbone contacts further stabilize the close side-by-side helical packing. The structure indicates the extent of RNA packing required for the function of large ribozymes, the spliceosome, and the ribosome.
==About this Structure==
==About this Structure==
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1GID is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with MG and NCO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GID OCA].
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1GID is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=NCO:'>NCO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GID OCA].
==Reference==
==Reference==
Crystal structure of a group I ribozyme domain: principles of RNA packing., Cate JH, Gooding AR, Podell E, Zhou K, Golden BL, Kundrot CE, Cech TR, Doudna JA, Science. 1996 Sep 20;273(5282):1678-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8781224 8781224]
Crystal structure of a group I ribozyme domain: principles of RNA packing., Cate JH, Gooding AR, Podell E, Zhou K, Golden BL, Kundrot CE, Cech TR, Doudna JA, Science. 1996 Sep 20;273(5282):1678-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8781224 8781224]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Cate, J.H.]]
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[[Category: Cate, J H.]]
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[[Category: Cech, T.R.]]
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[[Category: Cech, T R.]]
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[[Category: Doudna, J.A.]]
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[[Category: Doudna, J A.]]
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[[Category: Golden, B.L.]]
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[[Category: Golden, B L.]]
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[[Category: Gooding, A.R.]]
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[[Category: Gooding, A R.]]
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[[Category: Kundrot, C.E.]]
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[[Category: Kundrot, C E.]]
[[Category: Podell, E.]]
[[Category: Podell, E.]]
[[Category: Zhou, K.]]
[[Category: Zhou, K.]]
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[[Category: rna]]
[[Category: rna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:22:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:25 2008''

Revision as of 10:50, 21 February 2008


1gid, resolution 2.500Å

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CRYSTAL STRUCTURE OF A GROUP I RIBOZYME DOMAIN: PRINCIPLES OF RNA PACKING

Overview

Group I self-splicing introns catalyze their own excision from precursor RNAs by way of a two-step transesterification reaction. The catalytic core of these ribozymes is formed by two structural domains. The 2.8-angstrom crystal structure of one of these, the P4-P6 domain of the Tetrahymena thermophila intron, is described. In the 160-nucleotide domain, a sharp bend allows stacked helices of the conserved core to pack alongside helices of an adjacent region. Two specific long-range interactions clamp the two halves of the domain together: a two-Mg2+-coordinated adenosine-rich corkscrew plugs into the minor groove of a helix, and a GAAA hairpin loop binds to a conserved 11-nucleotide internal loop. Metal- and ribose-mediated backbone contacts further stabilize the close side-by-side helical packing. The structure indicates the extent of RNA packing required for the function of large ribozymes, the spliceosome, and the ribosome.

About this Structure

1GID is a Protein complex structure of sequences from [1] with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a group I ribozyme domain: principles of RNA packing., Cate JH, Gooding AR, Podell E, Zhou K, Golden BL, Kundrot CE, Cech TR, Doudna JA, Science. 1996 Sep 20;273(5282):1678-85. PMID:8781224

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