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Literature summary for 1.14.99.65 extracted from

  • Makris, T.M.; Knoot, C.J.; Wilmot, C.M.; Lipscomb, J.D.
    Structure of a dinuclear iron cluster-containing beta-hydroxylase active in antibiotic biosynthesis (2013), Biochemistry, 52, 6662-6671 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
to 2.7 A resolution. The C-terminal domain has the alphabetabetaalpha fold of the metallo-beta-lactamase superfamily. The N-terminal domain facilitates dimerization, and likely serves additional roles in nonribosomal peptide synthetase recognition and the regulation of O2 activation Streptomyces venezuelae

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the diiron cluster bound in the C-terminal domain is coordinated by an acetate, three His residues, two Asp residues, one Glu residue, and a bridging oxo moiety Streptomyces venezuelae

Organism

Organism UniProt Comment Textmining
Streptomyces venezuelae F2RB80
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Streptomyces venezuelae DSM 40230 F2RB80
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Synonyms

Synonyms Comment Organism
cmlA
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Streptomyces venezuelae