3EE4

R2-like ligand binding Mn/Fe oxidase from M. tuberculosis

Summary for 3EE4

• Entry DOI: 10.2210/pdb3ee4/pdb
• Descriptor: Probable ribonucleoside-diphosphate reductase, MYRISTIC ACID, MANGANESE (III) ION, ... (5 entities in total)
• Functional Keywords: manganese, iron, diiron, carboxylate, oxidase, r2, ligand, cavity, monooxygenase, oxidoreductase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 37124.37

Authors

Andersson, C.S.,Jones, T.A.,Hogbom, M. (deposition date: 2008-09-04, release date: 2009-04-07, Last modification date: 2024-11-20)

Primary citation

Andersson, C.S.
A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold
Proc.Natl.Acad.Sci.Usa, 106:5633-5638, 2009

PubMed Abstract: 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.

PubMed: 19321420
DOI: 10.1073/pnas.0812971106

Experimental method

X-RAY DIFFRACTION (1.9 Å)