5MGY

Crystal structure of Pseudomonas stutzeri flavinyl transferase ApbE, apo form

Summary for 5MGY

• Entry DOI: 10.2210/pdb5mgy/pdb
• Descriptor: FAD:protein FMN transferase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: fad binding protein flavinyl transferase, protein binding
• Biological source: Pseudomonas stutzeri ATCC 14405 = CCUG 16156
• Total number of polymer chains: 8
• Total formula weight: 288332.50

Authors

Zhang, L.,Trncik, C.,Andrade, S.L.A.,Einsle, O. (deposition date: 2016-11-22, release date: 2016-12-14, Last modification date: 2024-11-13)

Primary citation

Zhang, L.,Trncik, C.,Andrade, S.L.,Einsle, O.
The flavinyl transferase ApbE of Pseudomonas stutzeri matures the NosR protein required for nitrous oxide reduction.
Biochim. Biophys. Acta, 1858:95-102, 2016

PubMed Abstract: The copper-containing enzyme nitrous oxide reductase (NOR) catalyzes the transformation of nitrous oxide (NO) to dinitrogen (N) in microbial denitrification. Several accessory factors are essential for assembling the two copper sites Cu and Cu, and for maintaining the activity. In particular, the deletion of either the transmembrane iron-sulfur flavoprotein NosR or the periplasmic protein NosX, a member of the ApbE family, abolishes NO respiration. Here we demonstrate through biochemical and structural studies that the ApbE protein from Pseudomonas stutzeri, where the nosX gene is absent, is a monomeric FAD-binding protein that can serve as the flavin donor for NosR maturation via covalent flavinylation of a threonine residue. The flavin transfer reaction proceeds both in vivo and in vitro to generate post-translationally modified NosR with covalently bound FMN. Only FAD can act as substrate and the reaction requires a divalent cation, preferably Mg that was also present in the crystal structure. In addition, the reaction is species-specific to a certain extent.

PubMed: 27864152
DOI: 10.1016/j.bbabio.2016.11.008

Experimental method

X-RAY DIFFRACTION (2.6 Å)