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Literature summary for 1.1.2.3 extracted from

  • Xia, Z.X.; Mathews, F.S.
    Molecular structure of flavocytochrome b2 at 2.4 A resolution (1990), J. Mol. Biol., 212, 837-863.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of flavocytochrome b2 solved at 3.0 A resolution by the method of multiple isomorphous replacement with anomalous scattering Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
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Subunits

Subunits Comment Organism
tetramer
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Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
flavocytochrome b2
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Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
cytochrome each subunit of the tetramer is composed of two domains, one binding a heme and the other an FMN prosthetic group. The cytochrome domain consists of residues 1 to 99 Saccharomyces cerevisiae
FMN each subunit of the tetramer is composed of two domains, one binding a heme and the other an FMN prosthetic group. The flavin binding domain contains a parallel beta8alpha8 barrel structure and is composed of residues 100 to 486. The FMN moiety, which is located at the C-terminal end of the central beta-barrel, is mostly sequestered from solvent. It forms hydrogen bond interactions with main- and side-chain atoms from six of the eight beta-strands. The interaction of Lys349 with atoms N-1 and O-2 of the flavin ring is probably responsible for stabilization of the anionic form of the flavin semiquinone and hydroquinone and enhancing the reactivity of atom N-5 toward sulfite. The binding of pyruvate at the active site in subunit 2 is stabilized by interaction of its carboxylate group with the side-chain atoms of Arg376 and Tyr143. Residues His373 and Tyr254 interact with the keto-oxygen atom and are involved in catalysis. In contrast, four water molecules occupy the substrate-binding site in subunit 1 and Tyr143 forms a hydrogen bond to the ordered heme propionate group. Otherwise the two flavin-binding domains are identical within experimental error Saccharomyces cerevisiae