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Literature summary for 6.6.1.1 extracted from

  • Sirijovski, N.; Lundqvist, J.; Rosenbaeck, M.; Elmlund, H.; Al-Karadaghi, S.; Willows, R.D.; Hansson, M.
    Substrate-binding model of the chlorophyll biosynthetic magnesium chelatase BchH subunit (2008), J. Biol. Chem., 283, 11652-11660.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
subunit BchH, at 25 A resolution. The apo structure contains three major lobe-shaped domains connected at a single point with additional densities at the tip of two lobes termed the thumb and finger. The substrate-bound BchH complex BchH Proto shows a distinct conformational change in the thumb and finger subdomains. Prolonged proteolysis of native apo-BchH produces a stable C-terminal fragment of 45 kDa, and protoporphyrin protects the full-length polypeptide from degradation Rhodobacter capsulatus

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
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