Literature summary for 1.17.4.4 extracted from

Liu, S.; Cheng, W.; Fowle Grider, R.; Shen, G.; Li, W.
Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer (2014), Nat. Commun., 5, 3110 .

Cloned(Commentary)

Cloned (Comment)	Organism
mutant enzymes C50A and C212A are both expressed in a Escherichia coli BL21(DE3)	Synechococcus sp. JA-2-3B'a(2-13)

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting-drop vapor-diffusion method, the structure of the mutant enzyme Cys50Ala at 2.8 A resolution allows a detailed analysis of an intramembrane enzyme that generates disulfide bonds. In the active site, a continuous electron density connects the thiol group of Cys133 with the C1 atom of the quinone ring. The Cys212Ala structure suggests that the transfer of electrons to the active site is an one-electron process	Synechococcus sp. JA-2-3B'a(2-13)

Crystallization (Comment)

Organism

sitting-drop vapor-diffusion method, the structure of the mutant enzyme Cys50Ala at 2.8 A resolution allows a detailed analysis of an intramembrane enzyme that generates disulfide bonds. In the active site, a continuous electron density connects the thiol group of Cys133 with the C1 atom of the quinone ring. The Cys212Ala structure suggests that the transfer of electrons to the active site is an one-electron process

Synechococcus sp. JA-2-3B'a(2-13)

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	intramembrane enzyme	Synechococcus sp. JA-2-3B'a(2-13)	16020	-

Organism

Organism	UniProt	Comment	Textmining
Synechococcus sp. JA-2-3B'a(2-13)	Q2JJF6	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Synechococcus sp. JA-2-3B'a(2-13)

Source Tissue

Source Tissue	Comment	Organism	Textmining

Synonyms

Synonyms	Comment	Organism
vitamin K epoxide reductase	-	Synechococcus sp. JA-2-3B'a(2-13)
VKOR	-	Synechococcus sp. JA-2-3B'a(2-13)

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Release 2023.1 (January 2023)