1g0u

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(New page: 200px<br /><applet load="1g0u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g0u, resolution 2.40&Aring;" /> '''A GATED CHANNEL INTO...)
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[[Image:1g0u.jpg|left|200px]]<br /><applet load="1g0u" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1g0u.jpg|left|200px]]<br /><applet load="1g0u" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g0u, resolution 2.40&Aring;" />
caption="1g0u, resolution 2.40&Aring;" />
'''A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE'''<br />
'''A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE'''<br />
==Overview==
==Overview==
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The core particle (CP) of the yeast proteasome is composed of four, heptameric rings of subunits arranged in a hollow, barrel-like structure., We report that the CP is autoinhibited by the N-terminal tails of the, outer (alpha) ring subunits. Crystallographic analysis showed that, deletion of the tail of the alpha 3-subunit opens a channel into the, proteolytically active interior chamber of the CP, thus derepressing, peptide hydrolysis. In the latent state of the particle, the tails prevent, substrate entry by imposing topological closure on the CP. Inhibition by, the alpha-subunit tails is relieved upon binding of the regulatory, particle to the CP to form the proteasome holoenzyme.
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The core particle (CP) of the yeast proteasome is composed of four heptameric rings of subunits arranged in a hollow, barrel-like structure. We report that the CP is autoinhibited by the N-terminal tails of the outer (alpha) ring subunits. Crystallographic analysis showed that deletion of the tail of the alpha 3-subunit opens a channel into the proteolytically active interior chamber of the CP, thus derepressing peptide hydrolysis. In the latent state of the particle, the tails prevent substrate entry by imposing topological closure on the CP. Inhibition by the alpha-subunit tails is relieved upon binding of the regulatory particle to the CP to form the proteasome holoenzyme.
==About this Structure==
==About this Structure==
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1G0U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G0U OCA].
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1G0U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0U OCA].
==Reference==
==Reference==
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[[Category: Bajorek, M.]]
[[Category: Bajorek, M.]]
[[Category: Finley, D.]]
[[Category: Finley, D.]]
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[[Category: Glickman, M.H.]]
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[[Category: Glickman, M H.]]
[[Category: Groll, M.]]
[[Category: Groll, M.]]
[[Category: Huber, R.]]
[[Category: Huber, R.]]
[[Category: Kohler, A.]]
[[Category: Kohler, A.]]
[[Category: Moroder, L.]]
[[Category: Moroder, L.]]
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[[Category: Rubin, D.M.]]
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[[Category: Rubin, D M.]]
[[Category: MG]]
[[Category: MG]]
[[Category: degradation]]
[[Category: degradation]]
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[[Category: ubiquitin]]
[[Category: ubiquitin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:36:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:46 2008''

Revision as of 10:44, 21 February 2008


1g0u, resolution 2.40Å

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A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE

Overview

The core particle (CP) of the yeast proteasome is composed of four heptameric rings of subunits arranged in a hollow, barrel-like structure. We report that the CP is autoinhibited by the N-terminal tails of the outer (alpha) ring subunits. Crystallographic analysis showed that deletion of the tail of the alpha 3-subunit opens a channel into the proteolytically active interior chamber of the CP, thus derepressing peptide hydrolysis. In the latent state of the particle, the tails prevent substrate entry by imposing topological closure on the CP. Inhibition by the alpha-subunit tails is relieved upon binding of the regulatory particle to the CP to form the proteasome holoenzyme.

About this Structure

1G0U is a Protein complex structure of sequences from Saccharomyces cerevisiae with as ligand. Active as Proteasome endopeptidase complex, with EC number 3.4.25.1 Full crystallographic information is available from OCA.

Reference

A gated channel into the proteasome core particle., Groll M, Bajorek M, Kohler A, Moroder L, Rubin DM, Huber R, Glickman MH, Finley D, Nat Struct Biol. 2000 Nov;7(11):1062-7. PMID:11062564

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