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3.4.25.1: proteasome endopeptidase complex

This is an abbreviated version!
For detailed information about proteasome endopeptidase complex, go to the full flat file.

Word Map on EC 3.4.25.1

Reaction

cleavage of peptide bonds with very broad specificity =

Synonyms

20 S proteasome, 206 proteasome, 20S CP, 20S protease core, 20S proteasome, 26 S proteasome, 26S protease, 26S proteasome, 26S proteasome complex, 27 kDa prosomal protein, 30 kDa prosomal protein, beta1-PF1404, c20S, Component Y8, constitutive proteasome 20S, EC 3.4.22.21, EC 3.4.24.5, EC 3.4.99.46, GPRO-28, HsBPROS26, HSN3, i20S, immunoproteasome 20S, ingensin, KIPase, large multicatalytic protease, macropain, multi-subunit protease complex, multicatalytic endopeptidase complex, Multicatalytic endopeptidase complex C7, multicatalytic protease, multicatalytic proteinase, p27K, PROS-27, PROS-30, PROS-Dm25, PROS-Dm28.1, PROS-Dm29, PROS-Dm35, Pros26.4, prosome, proteasome, proteasome 19S, proteasome 20S, Proteasome component C13, Proteasome component C2, Proteasome component C3, Proteasome component C5, Proteasome component C8, Proteasome component C9, Proteasome component DD4, Proteasome component DD5, Proteasome component pts1, proteasome subunit alpha-type 7-like, PSMA5, Psma8, RING12 protein, RN3, Scl1, SCL1 suppressor protein, SFRICE_003436, T20S, TAS-F22/FAFP98, TAS-G64, TCPR29, tricorn protease, tricorn proteinase, XC3

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.25 Threonine endopeptidases
                3.4.25.1 proteasome endopeptidase complex

Crystallization

Crystallization on EC 3.4.25.1 - proteasome endopeptidase complex

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified 20S protease core, X-ray diffraction structure determination and analysis
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in complex with carfilzomib, hanging drop vapor diffusion method, using 0.2 M sodium formate, 40% (w/v) 2-methyl-2,4-pentanediol, at 16°C
in complex with peptide KYFTGSKLWRSYYA, to 3 A resolution
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purified 20S protease core, X-ray diffraction structure determination and analysis
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structure of the human 20S proteasome core bound to substrate analogue inhibitor adamantaneacetyl-(6-aminohexanoyl)3-(leucyl)3-vinylmethyl-sulfone, at a resolution of around 3.5 A
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purified 20S protease core, X-ray diffraction structure determination and analysis
cryo-EM structures of the actively ATP-hydrolyzing, substrate-engaged 26S proteasome with four distinct motor conformations. Structures suggest a ubiquitin capture mechanism, in which mechanical pulling on the substrate by the AAA+ motor delivers ubiquitin modifications directly into the Rpn11 catalytic groove and accelerates isopeptide cleavage for efficient, cotranslocational deubiquitination. The substrate polypeptide traverses from the Rpn11 deubiquitinase, through the AAA+ motor, and into the core peptidase. The proteasomal motor thereby adopts staircase arrangements with five substrate-engaged subunits and one disengaged subunit. Four of the substrate-engaged subunits are ATP bound, whereas the subunit at the bottom of the staircase and the disengaged subunit are bound to ADP
enzyme core particle with the alpha7DELTAN mutation, hanging drop vapor diffusion method, using 0.1 M MES (pH 6.5), 50 mM magnesium acetate, and 14% (v/v) 2-methyl-2,4-pentanediol
hanging drop vapour diffusion method, structure of the 20S proteasome/TMC-95A complex
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in complex with bortezomib, hanging drop vapour diffusion method at 24°C in 30 mM MgOAc, 100 mM MES (pH 7.2), and 10% 2-methyl-2,4-pentanediol
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purified 20S protease core, X-ray diffraction structure determination and analysis
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vapor diffusion method
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the 20S proteasome core particle forms stable complexes with one or two dimers of assembly chaperones PAC1-PAC2 and activators PA28gamma, PA200 in Spodoptera frugiperda Sf9 cells. Spontaneous detachment of 19S RP from isolated 26S proteasomes leaves core particles at different stages in the gate opening
crystal structure of the enzyme in complex with the competitive inhibitor acetyl-Leu-Leu-norleucinal
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purified 20S protease core, X-ray diffraction structure determination and analysis
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single particle cryo-electron microscoppy