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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
2009-4-8
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-10984489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-11315567,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-11328804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-11459480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-12664163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-12797828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-14550940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-14557599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-15247479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-15772113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-15858259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-1650033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-16756507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-16817931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-16846225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-16906752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-17176061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-17525338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-17601579,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-17616152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-18358006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-18627173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-18656954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-19033467,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-2190093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-8255292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-8861937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-8994966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-8999792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-9335290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-9634230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19321420-9692970
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1091-6490
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
7
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pubmed:volume |
106
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5633-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2009
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pubmed:articleTitle |
A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold.
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pubmed:affiliation |
Stockholm Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences C4, SE-106 91 Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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