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A dynamic c terminal segment in the mycobacterium tuberculosis mn/fe r2lox protein can adopt a helical structure with possible functional consequences
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2012 (English)In: Chemistry and Biodiversity, ISSN 1612-1872, Vol. 9, no 9, 1981-1988 p.Article in journal (Refereed) Published
Abstract [en]

Mycobacterium tuberculosis R2-like ligand-binding oxidase (MtR2lox) belongs to a recently discovered group of proteins that are homologous to the ribonucleotide reductase R2 proteins. MtR2lox carries a heterodinuclear Mn/Fe cofactor and, unlike R2 proteins, a large ligand-binding cavity. A unique tyrosine-valine cross link is also found in the vicinity of the active site. To date, all known structures of R2 and R2lox proteins show a disordered C-terminal segment. Here, we present two new crystal forms of MtR2lox, revealing an ordered helical C-terminal. The ability of alternating between an ordered and disordered state agrees well with bioinformatic analysis of the protein sequence. Interestingly, ordering of the C-terminal helix shields a large positively charged patch on the protein surface, potentially used for interaction with other cellular components. We hypothesize that the dynamic C-terminal segment may be involved in control of protein function in vivo.

Place, publisher, year, edition, pages
2012. Vol. 9, no 9, 1981-1988 p.
Keyword [en]
Protein folding, Metalloproteins, Structural dynamics, Ribonucleotide reductases, Oxidases, X-Ray crystallography
National Category
Biochemistry and Molecular Biology Biophysics
URN: urn:nbn:se:su:diva-81820DOI: 10.1002/cbdv.201100428ISI: 000308715800029OAI: diva2:565513
Swedish Research Council, 2010-5061Swedish Foundation for Strategic Research


Available from: 2012-11-07 Created: 2012-11-01 Last updated: 2013-11-25Bibliographically approved

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Andersson, Charlotta S.Berthold, Catrine L.Högbom, Martin
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