PDBsum entry 6c3c

Biosynthetic protein

PDB id: 6c3c

Contents

Protein chains

365 a.a.

Ligands

EDO ×11

PEG ×2

EJ1 ×2

Waters ×1025

PDB id:

6c3c

Name:

Biosynthetic protein

Title:

Plp-dependent l-arginine hydroxylase rohp quinonoid i complex

Structure:

Uncharacterized protein. Chain: a, b. Engineered: yes

Source:

Streptomyces cattleya. Organism_taxid: 1003195. Strain: atcc 35852 / dsm 46488 / jcm 4925 / nbrc 14057 / nrrl 8057. Gene: scatt_03970. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008

Resolution:

1.50Å R-factor: 0.164 R-free: 0.187

Authors:

J.B.Hedges,K.S.Ryan

Key ref:

J.B.Hedges et al. (2018). Snapshots of the Catalytic Cycle of an O₂, Pyridoxal Phosphate-Dependent Hydroxylase. ACS Chem Biol, 13, 965-974. PubMed id: 29466666 DOI: 10.1021/acschembio.8b00039

Date:

09-Jan-18 Release date: 07-Mar-18

Protein chains

G8WNK6  (G8WNK6_STREN) -  Aminotransferase class I/classII domain-containing protein from Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057)

Seq: 368 a.a.

Struc: 365 a.a.

DOI no: 10.1021/acschembio.8b00039

ACS Chem Biol 13:965-974 (2018)

PubMed id: 29466666

Snapshots of the Catalytic Cycle of an O₂, Pyridoxal Phosphate-Dependent Hydroxylase.

J.B.Hedges, E.Kuatsjah, Y.L.Du, L.D.Eltis, K.S.Ryan.

ABSTRACT

Enzymes that catalyze hydroxylation of unactivated carbons normally contain heme and nonheme iron cofactors. By contrast, how a pyridoxal phosphate (PLP)-dependent enzyme could catalyze such a hydroxylation was unknown. Here, we investigate RohP, a PLP-dependent enzyme that converts l-arginine to ( S)-4-hydroxy-2-ketoarginine. We determine that the RohP reaction consumes oxygen with stoichiometric release of H₂O₂. To understand this unusual chemistry, we obtain ∼1.5 Å resolution structures that capture intermediates along the catalytic cycle. Our data suggest that RohP carries out a four-electron oxidation and a stereospecific alkene hydration to give the ( S)-configured product. Together with our earlier studies on an O₂, PLP-dependent l-arginine oxidase, our work suggests that there is a shared pathway leading to both oxidized and hydroxylated products from l-arginine.