3h4p: Difference between revisions

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<StructureSection load='3h4p' size='340' side='right'caption='[[3h4p]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
<StructureSection load='3h4p' size='340' side='right'caption='[[3h4p]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[3h4p]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. 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"><div style='overflow: auto; max-height: 3em;'>[[3h43|3h43]], [[3h4m|3h4m]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.1&#8491;</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'>[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'>[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>
<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>
== Function ==
== Function ==
[[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> 
[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>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h4p ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h4p ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:19481527</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3h4p" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43067]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Proteasome endopeptidase complex]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Finley, D]]
[[Category: Finley D]]
[[Category: Hu, M]]
[[Category: Hu M]]
[[Category: Jeffrey, P D]]
[[Category: Jeffrey PD]]
[[Category: Shi, Y]]
[[Category: Shi Y]]
[[Category: Tian, G]]
[[Category: Tian G]]
[[Category: Zhang, F]]
[[Category: Zhang F]]
[[Category: Zhang, P]]
[[Category: Zhang P]]
[[Category: Core particle]]
[[Category: Hydrolase]]
[[Category: Protease]]
[[Category: Proteasome]]
[[Category: Threonine protease]]

Latest revision as of 12:58, 21 February 2024

Proteasome 20S core particle from Methanocaldococcus jannaschiiProteasome 20S core particle from Methanocaldococcus jannaschii

Structural highlights

3h4p is a 28 chain structure with sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Evolutionary Conservation

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

See Also

References

  1. ↑ 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

3h4p, resolution 4.10Å

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