1grz
From Proteopedia
(New page: 200px<br /><applet load="1grz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1grz, resolution 5.0Å" /> '''A PREORGANIZED ACTIVE...) |
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| - | [[Image:1grz.gif|left|200px]]<br /><applet load="1grz" size=" | + | [[Image:1grz.gif|left|200px]]<br /><applet load="1grz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1grz, resolution 5.0Å" /> | caption="1grz, resolution 5.0Å" /> | ||
'''A PREORGANIZED ACTIVE SITE IN THE CRYSTAL STRUCTURE OF THE TETRAHYMENA RIBOZYME'''<br /> | '''A PREORGANIZED ACTIVE SITE IN THE CRYSTAL STRUCTURE OF THE TETRAHYMENA RIBOZYME'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Group I introns possess a single active site that catalyzes the two | + | Group I introns possess a single active site that catalyzes the two sequential reactions of self-splicing. An RNA comprising the two domains of the Tetrahymena thermophila group I intron catalytic core retains activity, and the 5.0 angstrom crystal structure of this 247-nucleotide ribozyme is now described. Close packing of the two domains forms a shallow cleft capable of binding the short helix that contains the 5' splice site. The helix that provides the binding site for the guanosine substrate deviates significantly from A-form geometry, providing a tight binding pocket. The binding pockets for both the 5' splice site helix and guanosine are formed and oriented in the absence of these substrates. Thus, this large ribozyme is largely preorganized for catalysis, much like a globular protein enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1GRZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http:// | + | 1GRZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GRZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Tetrahymena thermophila]] | [[Category: Tetrahymena thermophila]] | ||
| - | [[Category: Cech, T | + | [[Category: Cech, T R.]] |
| - | [[Category: Golden, B | + | [[Category: Golden, B L.]] |
| - | [[Category: Gooding, A | + | [[Category: Gooding, A R.]] |
| - | [[Category: Podell, E | + | [[Category: Podell, E R.]] |
[[Category: ribozyme structure]] | [[Category: ribozyme structure]] | ||
[[Category: rrna group i intron]] | [[Category: rrna group i intron]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:21 2008'' |
Revision as of 10:53, 21 February 2008
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A PREORGANIZED ACTIVE SITE IN THE CRYSTAL STRUCTURE OF THE TETRAHYMENA RIBOZYME
Overview
Group I introns possess a single active site that catalyzes the two sequential reactions of self-splicing. An RNA comprising the two domains of the Tetrahymena thermophila group I intron catalytic core retains activity, and the 5.0 angstrom crystal structure of this 247-nucleotide ribozyme is now described. Close packing of the two domains forms a shallow cleft capable of binding the short helix that contains the 5' splice site. The helix that provides the binding site for the guanosine substrate deviates significantly from A-form geometry, providing a tight binding pocket. The binding pockets for both the 5' splice site helix and guanosine are formed and oriented in the absence of these substrates. Thus, this large ribozyme is largely preorganized for catalysis, much like a globular protein enzyme.
About this Structure
1GRZ is a Protein complex structure of sequences from Tetrahymena thermophila. Full crystallographic information is available from OCA.
Reference
A preorganized active site in the crystal structure of the Tetrahymena ribozyme., Golden BL, Gooding AR, Podell ER, Cech TR, Science. 1998 Oct 9;282(5387):259-64. PMID:9841391
Page seeded by OCA on Thu Feb 21 12:53:21 2008
