6NX0

Crystal structure of the diheme peroxidase BthA from Burkholderia thailandensis E264

Summary for 6NX0

• Entry DOI: 10.2210/pdb6nx0/pdb
• Descriptor: Di-haem cytochrome c peroxidase family protein, HEME C, NITRATE ION, ... (6 entities in total)
• Functional Keywords: heme, peroxidase, diheme, oxidoreductase
• Biological source: Burkholderia thailandensis E264
• Total number of polymer chains: 1
• Total formula weight: 53045.69

Authors

Cohen, S.E.,Drennan, C.L. (deposition date: 2019-02-07, release date: 2019-03-20, Last modification date: 2024-11-13)

Primary citation

Rizzolo, K.,Cohen, S.E.,Weitz, A.C.,Lopez Munoz, M.M.,Hendrich, M.P.,Drennan, C.L.,Elliott, S.J.
A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state.
Nat Commun, 10:1101-1101, 2019

PubMed Abstract: Bacterial diheme peroxidases represent a diverse enzyme family with functions that range from hydrogen peroxide (HO) reduction to post-translational modifications. By implementing a sequence similarity network (SSN) of the bCCP_MauG superfamily, we present the discovery of a unique diheme peroxidase BthA conserved in all Burkholderia. Using a combination of magnetic resonance, near-IR and Mössbauer spectroscopies and electrochemical methods, we report that BthA is capable of generating a bis-Fe(IV) species previously thought to be a unique feature of the diheme enzyme MauG. However, BthA is not MauG-like in that it catalytically converts HO to water, and a 1.54-Å resolution crystal structure reveals striking differences between BthA and other superfamily members, including the essential residues for both bis-Fe(IV) formation and HO turnover. Taken together, we find that BthA represents a previously undiscovered class of diheme enzymes, one that stabilizes a bis-Fe(IV) state and catalyzes HO turnover in a mechanistically distinct manner.

PubMed: 30846684
DOI: 10.1038/s41467-019-09020-4

Experimental method

X-RAY DIFFRACTION (1.54 Å)