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1j2q

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Revision as of 11:09, 4 August 2021

20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus

Structural highlights

1j2q is a 14 chain structure with sequence from Arcfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1j2p
Activity:	Proteasome endopeptidase complex, with EC number 3.4.25.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PSA_ARCFU] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation (By similarity).[HAMAP-Rule:MF_00289_A] [PSB_ARCFU] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation (By similarity).[HAMAP-Rule:MF_02113_A]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j2q"

@@ Line 3: / Line 3: @@
 <StructureSection load='1j2q' size='340' side='right'caption='[[1j2q]], [[Resolution|resolution]] 2.83&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1j2q]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J2Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1j2q]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J2Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIB:2-ACETYLAMINO-4-METHYL-PENTANOIC+ACID+[1-(1-FORMYL-PENTYLCARBAMOYL)-3-METHYL-BUTYL]-AMIDE'>CIB</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIB:2-ACETYLAMINO-4-METHYL-PENTANOIC+ACID+[1-(1-FORMYL-PENTYLCARBAMOYL)-3-METHYL-BUTYL]-AMIDE'>CIB</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j2p|1j2p]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1j2p|1j2p]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2q OCA], [http://pdbe.org/1j2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j2q RCSB], [http://www.ebi.ac.uk/pdbsum/1j2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2q ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2q OCA], [https://pdbe.org/1j2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j2q RCSB], [https://www.ebi.ac.uk/pdbsum/1j2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2q ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PSA_ARCFU PSA_ARCFU]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation (By similarity).[HAMAP-Rule:MF_00289_A] [[http://www.uniprot.org/uniprot/PSB_ARCFU PSB_ARCFU]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation (By similarity).[HAMAP-Rule:MF_02113_A]
+[[https://www.uniprot.org/uniprot/PSA_ARCFU PSA_ARCFU]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation (By similarity).[HAMAP-Rule:MF_00289_A] [[https://www.uniprot.org/uniprot/PSB_ARCFU PSB_ARCFU]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation (By similarity).[HAMAP-Rule:MF_02113_A]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Proteasome|Proteasome]]
+*[[Proteasome 3D structures|Proteasome 3D structures]]
 == References ==
 <references/>

1j2q

From Proteopedia

Revision as of 11:09, 4 August 2021

20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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