Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain

MARTIN ARAN; CLARA SMAL; LEONARDO PELLIZA; MARIANA GALLO; LISANDRO OTERO; SEBASTIÁN KLINKE; FERNANDO A. GOLDBAUM; ESTEBAN ITHURRALDE; ANDRÉS BERCOVICH; WALTER MAC CORMACK; ADRIÁN TURJANSKI; DANIEL O. CICERO

Proteins: Structure, Function, and Bioinformatics

Wiley

Año: 2014 vol. 82 p. 3062 - 3078

1097-0134

The structure of the BA42 protein belonging to the Antarctic flavobacterium Bizionia argentinensis was determined by Nuclear Magnetic Resonance and X-ray crystallography. This is the first structure of a member of the PF04536 family comprised of a stand-alone TPM domain. The structure reveals a new topological variant of the four beta-strands constituting the central beat-sheet of the alpha-beta-alpha architecture and a double metal binding site stabilizing a pair of crossing loops, not observed in previous structures of proteins belonging to this family. BA42 shows differences in structure and dynamics in the presence or absence of bound metals. The affinity for divalent metal ions is close to that observed in proteins that modulate their activity as a function of metal concentration, anticipating a possible role for BA42.