A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold. Export

@article{citeulike:6081152, 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.}, author = {Andersson, Charlotta S. and H\"{o}gbom, Martin}, citeulike-article-id = {6081152}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0812971106}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/19321420}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=19321420}, day = {7}, doi = {10.1073/pnas.0812971106}, issn = {1091-6490}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {ribonucleotide\_reductase}, month = {April}, number = {14}, pages = {5633--5638}, posted-at = {2009-11-06 16:11:42}, priority = {2}, title = {A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold.}, url = {http://dx.doi.org/10.1073/pnas.0812971106}, volume = {106}, year = {2009} }

TY - JOUR ID - citeulike:6081152 L3 - citeulike-article-id:6081152 N2 - 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. IS - 14 JF - Proceedings of the National Academy of Sciences of the United States of America SN - 1091-6490 EP - 5638 TI - A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold. VL - 106 SP - 5633 KW - ribonucleotide_reductase AU - Andersson, Charlotta AU - Högbom, Martin PY - 2009/04/07/ UR - http://dx.doi.org/10.1073/pnas.0812971106 ER -