Literature summary for 7.4.2.5 extracted from

Vassylyev, D.G.; Mori, H.; Vassylyeva, M.N.; Tsukazaki, T.; Kimura, Y.; Tahirov, T.H.; Ito, K.
Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer (2006), J. Mol. Biol., 364, 248-258.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
2.8 A resolution crystal structure	Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-

Subunits

Subunits	Comment	Organism
dimer	TtSecA forms parallel (head-to-head) dimers that are reminiscent of open scissors. The dimer interface is abundant in bulky Arg and Lys side-chains from both subunits, which stack on one another to form a basic zipper that is highly conserved	Thermus thermophilus

Synonyms

Synonyms	Comment	Organism
translocation ATPase SecA	-	Thermus thermophilus
TtSecA	-	Thermus thermophilus

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Release 2023.1 (January 2023)