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oligomer
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homo-oligomer in the cytosol, hetero-oligomer on peroxisome membranes
?
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x * 104000, PEX6, SDS-PAGE
?
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x * 141000, PEX1, SDS-PAGE
?
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x * 110000, Pex6p, SDS-PAGE
?
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x * 120000, Pex1p, SDS-PAGE
heptamer
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7 * 147000, small-angle X-ray scattering, SAXS, analysis
heptamer
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7 * 147000, small-angle X-ray scattering, SAXS, analysis
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heterohexamer
Q9FNP1; Q8RY16
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heterohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, Pex1p/Pex6p forms a type II heterohexameric complex with two AAA+ rings (D1 ring, D2 ring) and large N-terminal domains positioned on top and aside of the double ring structure
heterohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, Pex1p/Pex6p forms a type II heterohexameric complex with two AAA+ rings (D1 ring, D2 ring) and large N-terminal domains positioned on top and aside of the double ring structure
heterohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, Pex1p/Pex6p forms a type II heterohexameric complex with two AAA+ rings (D1 ring, D2 ring) and large N-terminal domains positioned on top and aside of the double ring structure
heterohexamer
Pex1p and Pex6p interact and form a heterohexameric complex in a one-to-one ratio of both AAA-proteins
heterohexamer
the enzyme complex exhibts a unique double-ring structure, cryo-electron microscopy
heterohexamer
the Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits, structure analysis, overview
heterohexamer
trimers of dimers, the peroxisomal proteins Pex1 and Pex6 form a heterohexameric type II AAA+ ATPase complex. The heterohexamer forms a trimer of Pex1/6 dimers with a triangular geometry that is atypical for AAA+ complexes. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs
heterohexamer
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Pex1 and Pex6 form a single, heterohexameric type-2 AAA-ATPase motor
heterohexamer
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Pex1 and Pex6 forma heterohexamer composed of a trimer of Pex1/6 dimers
heterohexamer
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the ATPases Pex1p and Pex6p represent a heterohexameric enzyme complex
homohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, the enzyme combines its AAA+ ring with a C-terminal protease segment
homohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, the enzyme combines its AAA+ ring with a C-terminal protease segment
homohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, the enzyme combines its AAA+ ring with a C-terminal protease segment
homohexamer
AAA+ modules consist of an ASCE domain and a C-terminal attached C-domain. The ASCE domain harbors the Walker A (p-loop) and Walker B motifs as well as the Sensor 1 and arginine-fingers (Arg-finger) within the second region of homology (SRH). The Sensor 2 is located in the C-domain. Hexameric ring formation with ATP binding sides located between the interfaces of the AAA+ protomers, the enzyme combines its AAA+ ring with a C-terminal protease segment
additional information
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Pex1p and Pex6p are believed to form heterohexameric structures
additional information
since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins. Under ATP depletion, Pex6p remains at the peroxisomal membrane, whereas Pex1p is released to the cytosol, probably as homotrimeric version
additional information
since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins. Under ATP depletion, Pex6p remains at the peroxisomal membrane, whereas Pex1p is released to the cytosol, probably as homotrimeric version
additional information
since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins
additional information
since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins
additional information
the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789)
additional information
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the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789)
additional information
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the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789)
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additional information
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Pex1p and Pex6p are believed to form heterohexameric structures
additional information
when the yeast Pex1p-Pex6p complex disassembles under ATP depleting conditions, Pex1p adopts a homotrimeric conformation, while Pex6p is monomeric. Since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins
additional information
when the yeast Pex1p-Pex6p complex disassembles under ATP depleting conditions, Pex1p adopts a homotrimeric conformation, while Pex6p is monomeric. Since interaction of Pex1p and Pex6p strongly depends on accurate nucleotide binding, heterohexameric complex formation might be a reversible process, autoregulated by the ATPase cycle of the AAA+-peroxins