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| - | {{Large structure}}
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| | ==Proteasome 20S core particle from Methanocaldococcus jannaschii== | | ==Proteasome 20S core particle from Methanocaldococcus jannaschii== |
| - | <StructureSection load='3h4p' size='340' side='right' caption='[[3h4p]], [[Resolution|resolution]] 4.10Å' scene=''> | + | <StructureSection load='3h4p' size='340' side='right'caption='[[3h4p]], [[Resolution|resolution]] 4.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3h4p]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H4P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3h4p]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H4P FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h43|3h43]], [[3h4m|3h4m]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3h43|3h43]], [[3h4m|3h4m]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">psmA, MJ0591 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067]), psmB, MJ1237 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">psmA, MJ0591 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067]), psmB, MJ1237 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</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=3h4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h4p OCA], [http://pdbe.org/3h4p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h4p RCSB], [http://www.ebi.ac.uk/pdbsum/3h4p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h4p 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=3h4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h4p OCA], [https://pdbe.org/3h4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h4p RCSB], [https://www.ebi.ac.uk/pdbsum/3h4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h4p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | {{Large structure}} | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PSA_METJA PSA_METJA]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin-like activity.[HAMAP-Rule:MF_00289]<ref>PMID:10692374</ref> [[http://www.uniprot.org/uniprot/PSB_METJA PSB_METJA]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin-like activity.[HAMAP-Rule:MF_02113]<ref>PMID:10692374</ref> | + | [[https://www.uniprot.org/uniprot/PSA_METJA PSA_METJA]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin-like activity.[HAMAP-Rule:MF_00289]<ref>PMID:10692374</ref> [[https://www.uniprot.org/uniprot/PSB_METJA PSB_METJA]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin-like activity.[HAMAP-Rule:MF_02113]<ref>PMID:10692374</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Proteasome|Proteasome]] | + | *[[Proteasome 3D structures|Proteasome 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Atcc 43067]] | | [[Category: Atcc 43067]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Proteasome endopeptidase complex]] | | [[Category: Proteasome endopeptidase complex]] |
| | [[Category: Finley, D]] | | [[Category: Finley, D]] |
| Structural highlights
Function
[PSA_METJA] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin-like activity.[HAMAP-Rule:MF_00289][1] [PSB_METJA] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin-like activity.[HAMAP-Rule:MF_02113][2]
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
Eukaryotic proteasome consists of a core particle (CP), which degrades unfolded protein, and a regulatory particle (RP), which is responsible for recognition, ATP-dependent unfolding, and translocation of polyubiquitinated substrate protein. In the archaea Methanocaldococcus jannaschii, the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). Here, we report the crystal structures of essential elements of the archaeal proteasome: the CP, the ATPase domain of PAN, and a distal subcomplex that is likely the first to encounter substrate. The distal subcomplex contains a coiled-coil segment and an OB-fold domain, both of which appear to be conserved in the eukaryotic proteasome. The OB domains of PAN form a hexameric ring with a 13 A pore, which likely constitutes the outermost constriction of the substrate translocation channel. These studies reveal structural codes and architecture of the complete proteasome, identify potential substrate-binding sites, and uncover unexpected asymmetry in the RP of archaea and eukaryotes.
Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii.,Zhang F, Hu M, Tian G, Zhang P, Finley D, Jeffrey PD, Shi Y Mol Cell. 2009 May 14;34(4):473-84. PMID:19481527[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wilson HL, Ou MS, Aldrich HC, Maupin-Furlow J. Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome. J Bacteriol. 2000 Mar;182(6):1680-92. PMID:10692374
- ↑ Wilson HL, Ou MS, Aldrich HC, Maupin-Furlow J. Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome. J Bacteriol. 2000 Mar;182(6):1680-92. PMID:10692374
- ↑ Zhang F, Hu M, Tian G, Zhang P, Finley D, Jeffrey PD, Shi Y. Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii. Mol Cell. 2009 May 14;34(4):473-84. PMID:19481527 doi:10.1016/j.molcel.2009.04.021
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