Literature summary for 1.18.6.2 extracted from

Sippel, D.; Einsle, O.
The structure of vanadium nitrogenase reveals an unusual bridging ligand (2017), Nat. Chem. Biol., 13, 956-960 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.35 A resolution. The protein contains an additional alpha-helical subunit not present in molybdenum nitrogenase. The FeV cofactor (FeVco) is a [V:7Fe:8S:C] cluster with a homocitrate ligand to vanadium. It lacks one sulfide ion compared to FeMoco that is replaced by a bridging ligand, likely a my-1,3-carbonate. It fits into a pocket within the protein that is obstructed in molybdenum nitrogenase	Azotobacter vinelandii

Crystallization (Comment)

Organism

to 1.35 A resolution. The protein contains an additional alpha-helical subunit not present in molybdenum nitrogenase. The FeV cofactor (FeVco) is a [V:7Fe:8S:C] cluster with a homocitrate ligand to vanadium. It lacks one sulfide ion compared to FeMoco that is replaced by a bridging ligand, likely a my-1,3-carbonate. It fits into a pocket within the protein that is obstructed in molybdenum nitrogenase

Azotobacter vinelandii

Organism

Organism	UniProt	Comment	Textmining
Azotobacter vinelandii	P16855	-	-

Synonyms

Synonyms	Comment	Organism
vnfD	-	Azotobacter vinelandii

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Release 2023.1 (January 2023)