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Literature summary extracted from

  • Djuranovic, S.; Hartmann, M.D.; Habeck, M.; Ursinus, A.; Zwickl, P.; Martin, J.; Lupas, A.N.; Zeth, K.
    Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases (2009), Mol. Cell, 34, 580-590.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.6.1.5 structure solved by multiple isomorphous replacement. One ARC-N monomer consists of two oligosaccharide-binding domains in tandem, the first from Ser80 to Tyr136 (OB1) and the second from Gly140 to Lys217 (OB2). The domains associate separately into hexameric rings Rhodococcus erythropolis
5.6.1.5 the structure is solved by molecular replacement with the N-terminal actinobacterial proteasomal ATPase oligosaccharide-binding domain OB1 as the search model. Each PAN-N monomer consists of an N-terminal coiled-coil helix and a C-terminal OB domain. The helices form two-strands coiled coils, while the OB domains associate into hexameric rings. Thus the structure can be described as a trimer of dimers Archaeoglobus fulgidus

Organism

EC Number Organism UniProt Comment Textmining
5.6.1.5 Archaeoglobus fulgidus O28303
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-
5.6.1.5 Rhodococcus erythropolis O50202
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-

Subunits

EC Number Subunits Comment Organism
5.6.1.5 hexamer ARC forms a hexameric ring which consist of an N-terminal coiled-coil and a C-terminal oligosaccharide-binding domain OB. In ARC-N, the OB-domains are duplicated and form separate rings. It can act as chaperone, preventing the aggregation of heterologous proteins in vitro, and this activity is preserved in various chimeras. The structure suggests a molecular mechanism for substrate processing based on concerted radial motions of the coiled coils relative to the rings Rhodococcus erythropolis
5.6.1.5 hexamer PAN forms a hexameric ring which subunits consist of an N-terminal coiled-coil and a C-terminal oligosaccharide-binding domain OB. PAN-N can act as chaperone. The structure suggests a molecular mechanism for substrate processing based on concerted radial motions of the coiled coils relative to the rings Archaeoglobus fulgidus
5.6.1.5 monomer each PAN-N monomer consists of an N-terminal coiled-coil helix and a C-terminal OB domain. The helices form two-strands coiled coils, while the OB domains associate into hexameric rings. Thus the structure can be described as a trimer of dimers Archaeoglobus fulgidus
5.6.1.5 monomer one ARC-N monomer consists of two oligosaccharide-binding domains in tandem, the first from Ser80 to Tyr136 (OB1) and the second from Gly140 to Lys217 (OB2). The domains associate separately into hexameric rings Rhodococcus erythropolis

Synonyms

EC Number Synonyms Comment Organism
5.6.1.5 actinobacterial proteasomal ATPase ARC
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 Rhodococcus erythropolis
5.6.1.5 ARC-N N-terminal actinobacterial proteasomal ATPase Rhodococcus erythropolis
5.6.1.5 archaeal proteasomal ATPase PAN
-
 Archaeoglobus fulgidus
5.6.1.5 PAN-N N-terminal archaeal proteasomal ATPase Archaeoglobus fulgidus