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Literature summary for 1.7.2.2 extracted from

  • Polyakov, K.M.; Boyko, K.M.; Tikhonova, T.V.; Slutsky, A.; Antipov, A.N.; Zvyagilskaya, R.A.; Popov, A.N.; Bourenkov, G.P.; Lamzin, V.S.; Popov, V.O.
    High-resolution structural analysis of a novel octaheme cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens (2009), J. Mol. Biol., 389, 846-862.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
apoenzyme and its complexes with the substrate nitrite and the inhibitor azide. The subunit of NiR consists of the N-terminal domain which has an unique fold and contains three hemes and the catalytic C-terminal domain which hosts the remaining five hemes. The complete set of eight hemes forms a spatial pattern characteristic of other multiheme proteins, including structurally characterized octaheme cytochromes. The catalytic machinery comprises the lysine residue at the proximal position of the catalytic heme, the catalytic triad of tyrosine, histidine, and arginine at the distal side, channels for the substrate and product transport with a characteristic gradient of electrostatic potential, and, two conserved Ca2+-binding sites. In addition, the enzyme has a covalent bond between the catalytic tyrosine and the adjacent cysteine and an unusual topography of the product channels that open into the void interior space of the protein hexamer Thioalkalivibrio nitratireducens

Organism

Organism UniProt Comment Textmining
Thioalkalivibrio nitratireducens Q5F2I3
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