Literature summary for 1.14.99.65 extracted from

Jasniewski, A.J.; Knoot, C.J.; Lipscomb, J.D.; Que, L.
A carboxylate shift regulates dioxygen activation by the diiron nonheme beta-hydroxylase CmlA upon binding of a substrate-loaded nonribosomal peptide synthetase (2016), Biochemistry, 55, 5818-5831 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure in the diferrous state. Formation of the active diferrous state CmlA-CmlP-L-p-aminophenylalanine complex converts at least one iron of the clusters from six- to five-coordinate by changing a bidentately bound amino acid carboxylate to monodentate on Fe1. The only bidentate carboxylate is residue E377	Streptomyces venezuelae

Protein Variants

Protein Variants	Comment	Organism
E377D	variant E377D shows only monodentate carboxylate coordination. Reduced E377D reacts rapidly with O2, showing loss of regulation. The mutant fails to catalyze hydroxylation	Streptomyces venezuelae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	the active site of CmlA contains a dinuclear iron cluster that is reduced to the diferrous state to initiate O2 activation	Streptomyces venezuelae

Organism

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

Synonyms

Synonyms	Comment	Organism
cmlA	-	Streptomyces venezuelae

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Release 2023.1 (January 2023)