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A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
2009 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 106, no 14, 5633-5638 p.Article in journal (Refereed) Published
Abstract [en]

Chlamydia trachomatis R2c is the prototype for a recently discovered group of ribonucleotide reductase R2 proteins that use a heterodinuclear Mn/Fe redox cofactor for radical generation and storage. Here, we show that the Mycobacterium tuberculosis protein Rv0233, an R2 homologue and a potential virulence factor, contains the heterodinuclear manganese/iron-carboxylate cofactor but displays a drastic remodeling of the R2 protein scaffold into a ligand-binding oxidase. The first structural characterization of the heterodinuclear cofactor shows that the site is highly specific for manganese and iron in their respective positions despite a symmetric arrangement of coordinating residues. In this protein scaffold, the Mn/Fe cofactor supports potent 2-electron oxidations as revealed by an unprecedented tyrosine-valine crosslink in the active site. This wolf in sheep's clothing defines a distinct functional group among R2 homologues and may represent a structural and functional counterpart of the evolutionary ancestor of R2s and bacterial multicomponent monooxygenases.

Place, publisher, year, edition, pages
2009. Vol. 106, no 14, 5633-5638 p.
Keyword [en]
bioinorganic chemistry, diiron, manganese, monooxygenase, R2c
National Category
Biological Sciences
URN: urn:nbn:se:uu:diva-129129DOI: 10.1073/pnas.0812971106ISI: 000264967500034OAI: oai:DiVA.org:uu-129129DiVA: diva2:337706
Available from: 2010-08-09 Created: 2010-08-05 Last updated: 2010-08-09Bibliographically approved

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