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Literature summary for 1.3.1.33 extracted from

  • Moser, J.; Lange, C.; Krausze, J.; Rebelein, J.; Schubert, W.D.; Ribbe, M.W.; Heinz, D.W.; Jahn, D.
    Structure of ADP-aluminium fluoride-stabilized protochlorophyllide oxidoreductase complex (2013), Proc. Natl. Acad. Sci. USA, 110, 2094-2098.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.1.33

Crystallization (Commentary)

Crystallization (Comment) Organism
the X-ray crystallographic structure of the substrate-bound, ADP-aluminium fluoride-stabilized (ADP-AlF3-stabilized) transition state complex between the DPOR components L2 and (NB)2 from the marine cyanobacterium Prochlorococcus marinus is reported Prochlorococcus marinus

Protein Variants

Protein Variants Comment Organism
H394A mutant retains only a moderate activity which points to a critical role of this residue in the specific protonation at C-18, probably by positioning a water molecule at a distance of 3.2 A from C-18 above the ring Prochlorococcus marinus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
360000
-
-
 Prochlorococcus marinus

Organism

Organism UniProt Comment Textmining
Prochlorococcus marinus Q7VD39
-
-

Subunits

Subunits Comment Organism
octamer heterooctameric complex: subunits N and B are structurally homologous, generating a pseudo-2fold symmetry axis that is colinear with the molecular twofold axis of L2. Both [4Fe-4S] clusters are centered around this extended axis: the L2 cluster is symmetrically ligated by four cysteinyl ligands between the two subunits, whereas the NB cluster is asymmetrically ligated by three cysteine residues from N and one aspartate residue from B Prochlorococcus marinus

Synonyms

Synonyms Comment Organism
dark-operative protochlorophyllide oxidoreductase
-
 Prochlorococcus marinus
DPOR
-
 Prochlorococcus marinus