3oqt

Publication Abstract from PubMed

Dodecins (assembly of twelve monomers) are the smallest known flavoprotein with only 65-73 amino acids and are involved in binding and storage of flavins in archaea. Here we report the crystal structure of Rv1498A, a Mycobacterium tuberculosis dodecin. This bacterial dodecin structure is similar to that of other reported dodecins. Each monomer has a 3 stranded beta-sheet and an alpha-helix perpendicular to it. This protein has polyextreme (halophilic and thermophilic) properties. Interestingly, positively and negatively charged residues aggregate separately and do not seem to contribute to thermophilic and halophilic stability. We have examined the interactions that stabilize the Rv1498A dodecamer by preparing selected point mutants that break salt bridges and hydrophobic contacts, thereby leading to collapse of the assembly.

Structural and biophysical characterization of Mycobacterium tuberculosis dodecin Rv1498A.,Liu F, Xiong J, Kumar S, Yang C, Ge S, Li S, Xia N, Swaminathan K J Struct Biol. 2011 Jul;175(1):31-8. Epub 2011 Apr 24. PMID:21539921^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.