Literature summary for 1.12.98.1 extracted from

Mills, D.; Vitt, S.; Strauss, M.; Shima, S.; Vonck, J.
De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy (2013), eLife, 2013, e00218.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure determined by near-atomic resolution cryo-electron microscopy with and without bound substrate F420. The 1.2-MDa complex contains 12 copies of the heterotrimer, which form a spherical protein shell with a hollow core. There is strong electron density of the chains of metal clusters running parallel to the protein shell, and the F420-binding site is located at the end of the chain near the outside of the spherical structure	Methanothermobacter marburgensis

Crystallization (Comment)

Organism

structure determined by near-atomic resolution cryo-electron microscopy with and without bound substrate F420. The 1.2-MDa complex contains 12 copies of the heterotrimer, which form a spherical protein shell with a hollow core. There is strong electron density of the chains of metal clusters running parallel to the protein shell, and the F420-binding site is located at the end of the chain near the outside of the spherical structure

Methanothermobacter marburgensis

Organism

Organism	UniProt	Comment	Textmining
Methanothermobacter marburgensis	D9PYF9	-	-

Purification (Commentary)

Purification (Comment)	Organism
strictly anaerobic conditions	Methanothermobacter marburgensis

Synonyms

Synonyms	Comment	Organism
F420-reducing [NiFe]-hydrogenase	-	Methanothermobacter marburgensis
FRH	-	Methanothermobacter marburgensis

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Release 2023.1 (January 2023)