5HYM

3-Hydroxybenzoate 6-hydroxylase from Rhodococcus jostii in complex with phosphatidylinositol

Summary for 5HYM

• Entry DOI: 10.2210/pdb5hym/pdb
• Descriptor: Probable salicylate monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE, Phosphatidylinositol, ... (5 entities in total)
• Functional Keywords: flavoprotein, monooxygenase, phospholipid, rhodococcus, oxidoreductase
• Biological source: Rhodococcus jostii (strain RHA1)
• Total number of polymer chains: 1
• Total formula weight: 48656.37

Authors

Orru, R.,Montersino, S.,Mattevi, A.,van Berkel, W.J.H. (deposition date: 2016-02-01, release date: 2017-02-01, Last modification date: 2024-01-10)

Primary citation

Montersino, S.,Te Poele, E.,Orru, R.,Westphal, A.H.,Barendregt, A.,Heck, A.J.R.,van der Geize, R.,Dijkhuizen, L.,Mattevi, A.,van Berkel, W.J.H.
3-Hydroxybenzoate 6-Hydroxylase from Rhodococcus jostii RHA1 Contains a Phosphatidylinositol Cofactor.
Front Microbiol, 8:1110-1110, 2017

PubMed Abstract: 3-Hydroxybenzoate 6-hydroxylase (3HB6H, EC 1.13.14.26) is a FAD-dependent monooxygenase involved in the catabolism of aromatic compounds in soil microorganisms. 3HB6H is unique among flavoprotein hydroxylases in that it harbors a phospholipid ligand. The purified protein obtained from expressing the gene encoding 3HB6H from RHA1 in the host contains a mixture of phosphatidylglycerol and phosphatidylethanolamine, which are the major constituents of cytoplasmic membrane. Here, we purified 3HB6H (HB6H) produced in the host RHA#2 by employing a newly developed actinomycete expression system. Biochemical and biophysical analysis revealed that 3HB6H possesses similar catalytic and structural features as 3HB6H, but now contains phosphatidylinositol, which is a specific constituent of actinomycete membranes. Native mass spectrometry suggests that the lipid cofactor stabilizes monomer-monomer contact. Lipid analysis of 3HB6H from NCIMB 9867 (3HB6H) produced in supports the conclusion that 3HB6H enzymes have an intrinsic ability to bind phospholipids with different specificity, reflecting the membrane composition of their bacterial host.

PubMed: 28670303
DOI: 10.3389/fmicb.2017.01110

Experimental method

X-RAY DIFFRACTION (2.3 Å)