A dynamic c terminal segment in the mycobacterium tuberculosis mn/fe r2lox protein can adopt a helical structure with possible functional consequences
2012 (English)In: Chemistry and Biodiversity, ISSN 1612-1872, Vol. 9, no 9, 1981-1988 p.Article in journal (Refereed) Published
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.
Protein folding, Metalloproteins, Structural dynamics, Ribonucleotide reductases, Oxidases, X-Ray crystallography
Biochemistry and Molecular Biology Biophysics
IdentifiersURN: urn:nbn:se:su:diva-81820DOI: 10.1002/cbdv.201100428ISI: 000308715800029OAI: oai:DiVA.org:su-81820DiVA: diva2:565513
FunderSwedish Research Council, 2010-5061Swedish Foundation for Strategic Research