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Literature summary for 1.14.13.154 extracted from

  • Savino, C.; Montemiglio, L.C.; Sciara, G.; Miele, A.E.; Kendrew, S.G.; Jemth, P.; Gianni, S.; Vallone, B.
    Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate (2009), J. Biol. Chem., 284, 29170-29179.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
recombinant His-tagged EryK is overexpressed in the Escherichia coli BL21 Saccharopolyspora erythraea

Crystallization (Commentary)

Crystallization (Comment) Organism
vapor diffusion at 21°C, three crystal forms of EryK are obtained in different crystallization conditions: with His tag (His6-EryK) in low salt conditions, without tag (EryK) in high salt, and in complex with its substrate erythromycin D (ErD-EryK) Saccharopolyspora erythraea

Organism

Organism UniProt Comment Textmining
Saccharopolyspora erythraea P48635
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-

Subunits

Subunits Comment Organism
monomer
-
 Saccharopolyspora erythraea

Synonyms

Synonyms Comment Organism
EryK
-
 Saccharopolyspora erythraea

Cofactor

Cofactor Comment Organism Structure
cytochrome P-450 a heme-thiolate protein (P-450) Saccharopolyspora erythraea