PDBsum entry 4b69

Oxidoreductase

PDB id: 4b69

Contents

Protein chain

448 a.a.

Ligands

FAD

ORN

SO4

GOL ×3

Waters ×124

PDB id:

4b69

Name:

Oxidoreductase

Title:

A. Fumigatus ornithine hydroxylase (sida) bound to ornithine

Structure:

L-ornithine n5 monooxygenase. Chain: a. Synonym: l-ornithine n5-oxygenase. Engineered: yes

Source:

Aspergillus fumigatus. Organism_taxid: 5085. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

2.30Å R-factor: 0.220 R-free: 0.268

Authors:

S.Franceschini,M.Fedkenheuer,N.J.Vogelaar,H.H.Robinson,P.Sobrado, A.Mattevi

Key ref:

S.Franceschini et al. (2012). Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases. Biochemistry, 51, 7043-7045. PubMed id: 22928747

Date:

09-Aug-12 Release date: 03-Oct-12

Protein chain

E9QYP0  (SIDA_ASPFU) -  L-ornithine N(5)-monooxygenase from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

Seq: 501 a.a.

Struc: 448 a.a.

Enzyme reactions

• Enzyme class: E.C.1.14.13.196 - L-ornithine N(5)-monooxygenase [NAD(P)H].
• Reaction:
  1. L-ornithine + NADPH + O2 = N₅-hydroxy-L-ornithine + NADP⁺ + H2O
  2. L-ornithine + NADH + O2 = N₅-hydroxy-L-ornithine + NAD⁺ + H2O

L-ornithine (Bound ligand (Het Group name = ORN) corresponds exactly) + NADPH + O2 = N(5)-hydroxy-L-ornithine + NADP(+) + H2O

L-ornithine (Bound ligand (Het Group name = ORN) corresponds exactly) + NADH + O2 = N(5)-hydroxy-L-ornithine + NAD(+) + H2O

• Cofactor: FAD

FAD (Bound ligand (Het Group name = FAD) corresponds exactly)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Biochemistry 51:7043-7045 (2012)

PubMed id: 22928747

Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases.

S.Franceschini, M.Fedkenheuer, N.J.Vogelaar, H.H.Robinson, P.Sobrado, A.Mattevi.

ABSTRACT

SidA from the human pathogen Aspergillus fumigatus catalyzes the generation of N(5)-hydroxyornithine in the biosynthesis of siderophores, a reaction essential for virulence. The crystal structures of SidA in complex with ornithine and lysine reveal the geometry of the interactions among flavin, NADP(+), and the substrate amine group that underlie the hydroxylation reaction. The structural elucidation of the enzyme in complex with arginine provides insight into the role of electrostatics and hydrogen bonding in the mechanism of oxygen activation in this family of enzymes.