Unanticipated coordination of tris buffer to the Radical SAM cluster of the RimO methylthiotransferase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-06-03

AUTHORS

Thibaut Molle, Martin Clémancey, Jean-Marc Latour, Velavan Kathirvelu, Giuseppe Sicoli, Farhad Forouhar, Etienne Mulliez, Serge Gambarelli, Mohamed Atta

ABSTRACT

Radical SAM enzymes generally contain a [4Fe–4S]2+/1+ (RS cluster) cluster bound to the protein via the three cysteines of a canonical motif CxxxCxxC. The non-cysteinyl iron is used to coordinate SAM via its amino-carboxylate moiety. The coordination-induced proximity between the cluster acting as an electron donor and the adenosyl–sulfonium bond of SAM allows for the homolytic cleavage of the latter leading to the formation of the reactive 5′-deoxyadenosyl radical used for substrate activation. Most of the structures of Radical SAM enzymes have been obtained in the presence of SAM, and therefore, little is known about the situation when SAM is not present. In this report, we show that RimO, a methylthiotransferase belonging to the radical SAM superfamily, binds a Tris molecule in the absence of SAM leading to specific spectroscopic signatures both in Mössbauer and pulsed EPR spectroscopies. These data provide a cautionary note for researchers who work with coordinative unsaturated iron sulfur clusters. More... »

PAGES

549-557

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00775-016-1365-8

DOI

http://dx.doi.org/10.1007/s00775-016-1365-8

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1033392637

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27259294


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