5FFQ

ChuY: An Anaerobillin Reductase from Escherichia coli O157:H7

Summary for 5FFQ

• Entry DOI: 10.2210/pdb5ffq/pdb
• Descriptor: ShuY-like protein, PHOSPHATE ION, 1,4-BUTANEDIOL, ... (4 entities in total)
• Functional Keywords: nadph oxidoreductase, unknown function
• Biological source: Escherichia coli O157:H7
• Total number of polymer chains: 2
• Total formula weight: 43951.79

Authors

LaMattina, J.W.,Reedy, A.N.,Uy, K.G.,Lanzilotta, W.N. (deposition date: 2015-12-18, release date: 2017-01-11, Last modification date: 2023-09-27)

Primary citation

LaMattina, J.W.,Nix, D.B.,Lanzilotta, W.N.
Radical new paradigm for heme degradation in Escherichia coli O157:H7.
Proc. Natl. Acad. Sci. U.S.A., 113:12138-12143, 2016

PubMed Abstract: All of the heme-degrading enzymes that have been characterized to date require molecular oxygen as a cosubstrate. Escherichia coli O157:H7 has been shown to express heme uptake and transport proteins, as well as use heme as an iron source. This enteric pathogen colonizes the anaerobic space of the lower intestine in mammals, yet no mechanism for anaerobic heme degradation has been reported. Herein we provide evidence for an oxygen-independent heme-degradation pathway. Specifically, we demonstrate that ChuW is a radical S-adenosylmethionine methyltransferase that catalyzes a radical-mediated mechanism facilitating iron liberation and the production of the tetrapyrrole product we termed "anaerobilin." We further demonstrate that anaerobilin can be used as a substrate by ChuY, an enzyme that is coexpressed with ChuW in vivo along with the heme uptake machinery. Our findings are discussed in terms of the competitive advantage this system provides for enteric bacteria, particularly those that inhabit an anaerobic niche in the intestines.

PubMed: 27791000
DOI: 10.1073/pnas.1603209113

Experimental method

X-RAY DIFFRACTION (2 Å)