Literature summary for 1.3.7.6 extracted from

Dammeyer, T.; Hofmann, E.; Frankenberg-Dinkel, N.
Phycoerythrobilin synthase (PebS) of a marine virus. Crystal structures of the biliverdin complex and the substrate-free form (2008), J. Biol. Chem., 283, 27547-27554.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of substrate complex solved at 1.8- and 2.1 A resolution and of the substrate-free form at 1.55 A resolution. The overall folding reveals an alpha/beta/alpha-sandwich with similarity to the structure of phycocyanobilin:ferredoxin oxidoreductase. The substrate-binding site is located between the central beta-sheet and C-terminal alpha-helices. The substrate binding pocket shows a high flexibility. The substrate is either in a planar porphyrin-like conformation or in a helical conformation and is coordinated by a conserved aspartate/asparagine pair from the beta-sheet side. From the alpha-helix side, a conserved highlyflexible aspartate/proline pair is involved in substrate binding and presumably catalysis	Prochlorococcus phage P-SSM2

Crystallization (Comment)

Organism

structures of substrate complex solved at 1.8- and 2.1 A resolution and of the substrate-free form at 1.55 A resolution. The overall folding reveals an alpha/beta/alpha-sandwich with similarity to the structure of phycocyanobilin:ferredoxin oxidoreductase. The substrate-binding site is located between the central beta-sheet and C-terminal alpha-helices. The substrate binding pocket shows a high flexibility. The substrate is either in a planar porphyrin-like conformation or in a helical conformation and is coordinated by a conserved aspartate/asparagine pair from the beta-sheet side. From the alpha-helix side, a conserved highlyflexible aspartate/proline pair is involved in substrate binding and presumably catalysis

Prochlorococcus phage P-SSM2

Organism

Organism	UniProt	Comment	Textmining
Prochlorococcus phage P-SSM2	Q58MU6	-	-

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Release 2023.1 (January 2023)