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Structure of Archeabacterial 20S proteasome mutant D9S- PA26 complex

X-ray diffraction
1.9Å resolution
PDB entry 1yar coloured by chain, front view.
PDB entry 1yar coloured by chain, side view.
PDB entry 1yar coloured by chain, top view.
Source organisms:
Assembly composition:
hetero 42-mer (preferred)
Entry contents: 3 distinct polypeptide molecules

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Proteasome complex
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Multimeric state: hetero 42-mer
Accessible surface area: 308339.9 Å2
Buried surface area: 191747.97 Å2
Dissociation area: 8,323.43 Å2
Dissociation energy (ΔGdiss): 86.43 kcal/mol
Dissociation entropy (TΔSdiss): 19.97 kcal/mol
Symmetry number: 14
PDBe Complex ID: PDB-CPX-150393

Macromolecules

Proteasome subunit alpha
Chains: A, B, C, D, E, F, G
Length: 233 amino acids
Theoretical weight: 25.8 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P25156 (Residues: 1-233; Coverage: 100%)
Gene names: Ta1288, psmA
Pfam:
InterPro:
CATH: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
SCOP: Proteasome subunits
Proteasome subunit alpha in PDB entry 1yar, assembly 1, front view.
Proteasome subunit alpha in PDB entry 1yar, assembly 1, side view.
Proteasome subunit alpha in PDB entry 1yar, assembly 1, top view.
PDBe-KB: UniProt Coverage View: P25156  
123320406080100120140160180200220
 
100200MQQGQMAYSRAITVFSPDGRLFQVEYAREAVKKGSTALGMKFANGVLLISDKKVRSRLIEQNSIEKIQLIDDYVAAVTSGLVADARVLVDFARISAQQEKVTYGSLVNIENLVKRVADQMQQYTQYGGVRPYGVSLIFAGIDQIGPRLFDCDPAGTINEYKATAIGSGKDAVVSFLEREYKENLPEKEAVTLGIKALKSSLEEGEELKAPEIASITVGNKYRIYDQEEVKKFL
UniProt
P25156
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation
Molecule details ›

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Proteasome subunit beta
Chains: H, I, J, K, L, M, N
Length: 217 amino acids
Theoretical weight: 24 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P28061 (Residues: 1-211; Coverage: 100%)
Gene names: Ta0612, psmB
Pfam: Proteasome subunit
InterPro:
CATH: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
SCOP: Proteasome subunits
Proteasome subunit beta in PDB entry 1yar, assembly 1, front view.
Proteasome subunit beta in PDB entry 1yar, assembly 1, side view.
Proteasome subunit beta in PDB entry 1yar, assembly 1, top view.
PDBe-KB: UniProt Coverage View: P28061  
121720406080100120140160180200
 
100200MNQTLETGTTTVGITLKDAVIMATERRVTMENFIMHKNGKKLFQIDTYTGMTIAGLVGDAQVLVRYMKAELELYRLQRRVNMPIEAVATLLSNMLNQVKYMPYMVQLLVGGIDTAPHVFSIDAAGGSVEDIYASTGSGSPFVYGVLESQYSEKMTVDEGVDLVIRAISAAKQRDSASGGMIDVAVITRKDGYVQLPTDQIESRIRKLGLILHHHHHH
UniProt
P28061
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation
Molecule details ›

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Proteasome activator PA28 C-terminal domain-containing protein
Chains: O, P, Q, R, S, T, U
Length: 237 amino acids
Theoretical weight: 26.09 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9U8G2 (Residues: 2-231; Coverage: 100%)
Pfam: Proteasome activator PA28, C-terminal
InterPro:
CATH: Proteasome activator pa28, C-terminal domain
SCOP: Proteasome activator
Proteasome activator PA28 C-terminal domain-containing protein in PDB entry 1yar, assembly 1, front view.
Proteasome activator PA28 C-terminal domain-containing protein in PDB entry 1yar, assembly 1, side view.
Proteasome activator PA28 C-terminal domain-containing protein in PDB entry 1yar, assembly 1, top view.
PDBe-KB: UniProt Coverage View: Q9U8G2  
123720406080100120140160180200220
 
100200MHHHHHHPPKRAALIQNLRDSYTETSSFAVIEEWAAGTLQEIEGIAKAAAEAHGVIRNSTYGRAQAEKSPEQLLGVLQRYQDLCHNVYCQAETIRTVIAIRIPEHKEEDNLGVAVQHAVLKIIDELEIKTLGSGEKSGSGGAPTPIGMYALREYLSARSTVEDKLLGSVDAESGKTKGGSQSPSLLLELRQIDADFMLKVELATTHLSTMVRAVINAYLLNWKKLIQPRTGSDHMVS
UniProt
Q9U8G2
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces
Sequence conservation
Molecule details ›

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