3h4p

Proteasome 20S core particle from Methanocaldococcus jannaschii

spinqualitylabelsall models 3h4p, resolution 4.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. Related: 3h43, 3h4m Gene: psmA, MJ0591 (Methanocaldococcus jannaschii), psmB, MJ1237 (Methanocaldococcus jannaschii) Activity: Proteasome endopeptidase complex, with EC number 3.4.25.1 Resources: FirstGlance, OCA, RCSB, PDBsum Function [PSMA_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. [PSMB_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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Proteasome

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