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Structure paper

TitleA unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome.
Journal, issue, pagesNat Commun, Vol. 7, Page 10900-10900, Year 2016
Publish dateJul 31, 2015 (structure data deposition date)
AuthorsHuber, E.M. / Heinemeyer, W. / Li, X. / Arendt, C.S. / Hochstrasser, M. / Groll, M.
External linksNat Commun / PubMed:26964885
MethodsX-ray diffraction
Resolution2.3 - 2.9 Å
Structure data

PDB-5cz4:
Yeast 20S proteasome at 2.3 A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-5cz5:
Yeast 20S proteasome beta1-T1A mutant in complex with Carfilzomib
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5cz6:
Yeast 20S proteasome beta5-T1A mutant in complex with Syringolin A, propeptide expressed in trans
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-5cz7:
Yeast 20S proteasome beta5-T1A beta5-K81R double mutant in complex with Bortezomib, propeptide expressed in cis
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5cz8:
Yeast 20S proteasome beta5-L(-49)S-K33A mutant in complex with Carfilzomib
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5cz9:
Yeast 20S proteasome beta5-D17N mutant in complex with Carfilzomib; Propeptide expressed in trans
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-5cza:
Yeast 20S proteasome beta5-D166N mutant
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5d0s:
Yeast 20S proteasome beta5-D166N mutant in complex with Carfilzomib
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5d0t:
Yeast 20S proteasome beta5-D166N mutant in complex with MG132
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-5d0v:
Yeast 20S proteasome beta5-T1C mutant in complex with Carfilzomib
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-5d0w:
Yeast 20S proteasome beta5-T1S mutant
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5d0x:
Yeast 20S proteasome beta5-T1S mutant in complex with Bortezomib
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-5d0z:
Yeast 20S proteasome beta5-T1S mutant in complex with Carfilzomib
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-5fg7:
Yeast 20S proteasome beta2-T1A mutant
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-5fg9:
Yeast 20S proteasome beta2-T(-2)V mutant
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-5fga:
Yeast 20S proteasome beta5-K33A mutant (propeptide expressed in trans)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-5fgd:
Yeast 20S proteasome beta5-H(-2)L-T1A double mutant in complex with Carfilzomib
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5fge:
Yeast 20S proteasome beta5-H(-2)T-T1A double mutant in complex with Carfilzomib
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-5fgf:
Yeast 20S proteasome beta5-H(-2)A-T1A-K81R triple mutant in complex with Carfilzomib
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-5fgg:
Yeast 20S proteasome beta5-L(-49S)_D17N double mutant in complex with Carfilzomib
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-5fgh:
Yeast 20S proteasome beta5-K33A mutant (propeptide expressed in trans) in complex with MG132
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5fgi:
Yeast 20S proteasome beta1-T1A beta2-T1A double mutant in complex with Carfilzomib
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-5fhs:
Yeast 20S proteasome beta5-K33A mutant (propeptide expressed in trans) in complex with Carfilzomib
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-3BV:
N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide / medication, anticancer, inhibitor*YM

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-SRG:
(2S)-2-[[(2S)-1-[[(5S,8S,9E)-2,7-dioxo-5-propan-2-yl-1,6-diazacyclododeca-3,9-dien-8-yl]amino]-3-methyl-1-oxo-butan-2-yl]carbamoylamino]-3-methyl-butanoic acid

ChemComp-BO2:
N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE / medication, anticancer*YM

ChemComp-ALD:
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-hydroxy-4-methylpentan-2-yl]-L-leucinamide

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • synthetic construct (others)
  • saccharomyces cerevisiae s288c (yeast)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / HYDROLASE-HYDROLASE complex / Ubiquitin-Degradation System / Proteasome / NTN-Hydrolase / Thr-Protease / HYDROLASE-HYDROLASE INHIBITOR complex / Mutant / Inhibitor / Binding Analysis / HYDROLASE complex

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