Literature summary for 3.4.24.B20 extracted from

Uthoff, M.; Baumann, U.
Conformational flexibility of pore loop-1 gives insights into substrate translocation by the AAA+ protease FtsH (2018), J. Struct. Biol., 204, 199-206 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of a transmembrane helix-lacking FtsH construct from Aquifex aeolicus, at 2.9 A and 3.3 A resolution in space groups R32 and P312, respectively. In both structures, the FtsH hexamer is created from two different subunits of the asymmetric unit by the threefold symmetry of the crystals. All subunits are loaded with ADP. Within the ATPase cycle while the whole subunit switches from the opened to the closed state, pore loop-1 interacts with the substrate and translocates it into the proteolytic chamber	Aquifex aeolicus

Crystallization (Comment)

Organism

structures of a transmembrane helix-lacking FtsH construct from Aquifex aeolicus, at 2.9 A and 3.3 A resolution in space groups R32 and P312, respectively. In both structures, the FtsH hexamer is created from two different subunits of the asymmetric unit by the threefold symmetry of the crystals. All subunits are loaded with ADP. Within the ATPase cycle while the whole subunit switches from the opened to the closed state, pore loop-1 interacts with the substrate and translocates it into the proteolytic chamber

Aquifex aeolicus

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	O67077	-	-

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Release 2023.1 (January 2023)