Literature summary for 7.1.1.1 extracted from

Padayatti, P.S.; Leung, J.H.; Mahinthichaichan, P.; Tajkhorshid, E.; Ishchenko, A.; Cherezov, V.; Soltis, S.M.; Jackson, J.B.; Stout, C.D.; Gennis, R.B.; Zhang, Q.
Critical role of water molecules in proton translocation by the membrane-bound transhydrogenase (2017), Structure, 25, 1111-1119 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
2.2 A crystal structure of the transmembrane domain at pH 6.5. Presence of transient water flows across a narrow pore and a hydrophobic region in the middle of the membrane channel with key residues His42alpha2 (chain A) being protonated and Thr214beta (chain B) displaying a conformational change, respectively, to gate the channel access to both cytoplasmic and periplasmic chambers	Thermus thermophilus

Protein Variants

Protein Variants	Comment	Organism
T214A	mutation in chain B, 3-5% residual activity	Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	Q72GR9	-	-
Thermus thermophilus DSM 7039	Q72GR9	-	-

Synonyms

Synonyms	Comment	Organism
proton-translocating NAD(P)(+) transhydrogenase	-	Thermus thermophilus
TT_C1779	-	Thermus thermophilus

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Release 2023.1 (January 2023)