Literature summary for 5.6.1.5 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.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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
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

Crystallization (Comment)

Organism

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

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

Organism	UniProt	Comment	Textmining
Archaeoglobus fulgidus	O28303	-	-
Rhodococcus erythropolis	O50202	-	-

Subunits

Subunits	Comment	Organism
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
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
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
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

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