1j2p: Difference between revisions

Revision as of 14:18, 21 February 2008

alpha-ring from the proteasome from archaeoglobus fulgidus

OverviewOverview

The 20S proteasome (core particle, CP) is a multifunctional protease complex and composed of four heptameric subunit rings arranged in a hollow, barrel-shaped structure. Here, we report the crystal structure of the CP from Archaeoglobus fulgidus at 2.25A resolution. The analysis of the structure of early and late assembly intermediates of this CP gives new insights in the maturation of archaebacterial CPs and indicates similarities to assembly intermediates observed in eukaryotes. We also show a striking difference in mechanism and regulation of substrate access between eukaryotic and archaebacterial 20S proteasomes. While eukaryotic CPs are auto-inhibited by the N-terminal tails of the outer alpha-ring by imposing topological closure with a characteristic sequence motif (YDR-motif) and show regulatory gating this segment is disordered in the CP and differently structured in the alpha(7)-sub-complex of A.fulgidus leaving a pore leading into the particle with a diameter of 13A. Mutagenesis and functional studies indicate the absence of regulatory gating in the archaeal 20S proteasome.

About this StructureAbout this Structure

1J2P is a Single protein structure of sequence from Archaeoglobus fulgidus. Active as Proteasome endopeptidase complex, with EC number 3.4.25.1 Full crystallographic information is available from OCA.

ReferenceReference

Investigations on the maturation and regulation of archaebacterial proteasomes., Groll M, Brandstetter H, Bartunik H, Bourenkow G, Huber R, J Mol Biol. 2003 Mar 14;327(1):75-83. PMID:12614609

Page seeded by OCA on Thu Feb 21 13:18:17 2008

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OCA

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-[[Image:1j2p.gif|left|200px]]<br /><applet load="1j2p" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1j2p.gif|left|200px]]<br /><applet load="1j2p" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1j2p, resolution 2.60&Aring;" />
 '''alpha-ring from the proteasome from archaeoglobus fulgidus'''<br />
 ==Overview==
-The 20S proteasome (core particle, CP) is a multifunctional protease, complex and composed of four heptameric subunit rings arranged in a, hollow, barrel-shaped structure. Here, we report the crystal structure of, the CP from Archaeoglobus fulgidus at 2.25A resolution. The analysis of, the structure of early and late assembly intermediates of this CP gives, new insights in the maturation of archaebacterial CPs and indicates, similarities to assembly intermediates observed in eukaryotes. We also, show a striking difference in mechanism and regulation of substrate access, between eukaryotic and archaebacterial 20S proteasomes. While eukaryotic, CPs are auto-inhibited by the N-terminal tails of the outer alpha-ring by, imposing topological closure with a characteristic sequence motif, (YDR-motif) and show regulatory gating this segment is disordered in the, CP and differently structured in the alpha(7)-sub-complex of A.fulgidus, leaving a pore leading into the particle with a diameter of 13A., Mutagenesis and functional studies indicate the absence of regulatory, gating in the archaeal 20S proteasome.
+The 20S proteasome (core particle, CP) is a multifunctional protease complex and composed of four heptameric subunit rings arranged in a hollow, barrel-shaped structure. Here, we report the crystal structure of the CP from Archaeoglobus fulgidus at 2.25A resolution. The analysis of the structure of early and late assembly intermediates of this CP gives new insights in the maturation of archaebacterial CPs and indicates similarities to assembly intermediates observed in eukaryotes. We also show a striking difference in mechanism and regulation of substrate access between eukaryotic and archaebacterial 20S proteasomes. While eukaryotic CPs are auto-inhibited by the N-terminal tails of the outer alpha-ring by imposing topological closure with a characteristic sequence motif (YDR-motif) and show regulatory gating this segment is disordered in the CP and differently structured in the alpha(7)-sub-complex of A.fulgidus leaving a pore leading into the particle with a diameter of 13A. Mutagenesis and functional studies indicate the absence of regulatory gating in the archaeal 20S proteasome.
 ==About this Structure==
-J2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. 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=1J2P OCA].
+J2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. 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=1J2P OCA].
 ==Reference==
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 [[Category: proteasome]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:53:07 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:17 2008''