IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
? Discovering function from protein structure: The BA42 protein from the antarctic bacteria B. Argentinensis is a novel phosphatase.
Autor/es:
CLARA SMAL; MARTÍN ARAN; LEONARDO PELLIZZA; MARIANA GALLO; ANDRES BERCOVICH; WALTER P. MAC CORMACK; ADRIAN G. TURJANSKI; DANIEL O. CICERO
Lugar:
Pisa
Reunión:
Congreso; XLI National Meeting of the GIDRM; 2012
Institución organizadora:
GIDRM
Resumen:
The bacteria Bizionia argentinensis sp. Nov (BA) was isolated from surface seawater in Antarctica and the phylogenetic
analysis showed that it belongs to a novel species of the genus Bizionia [1]. The BA
genome was recently decoded [2] and constitutes a
relevant source for the discovery of new proteins showing biological activity
in extreme conditions of low temperatures. In particular, we are interested in
those proteins for which function cannot be inferred solely on sequence, and
for which structural homologues are not available. To study this type of proteins, a network of
NMR Laboratories was created, giving birth to the Extremophiles Structural
Genomics consortium (ESG). ESG includes the NMR Laboratories of Fundación
Instituto Leloir, Buenos Aires, Argentina, Verona University and Parma
University, Italy.
In this
work we present the first structure of a BA
protein of unknown function, the BA42 protein, codified by the ORF 00042 contig
3 [3]. BA42 presents significant
sequence identity with a PfamA family, DUF477 (Domain of Unknown Function). Proteins
of this family are found both in eukarya and eubacteria. The three-dimensional
structure consists in a three-layer sandwich with three a-helices in the upper layer,
four b-sheets in
the middle layer, and one a-helix
in the lower layer. Using the DALI server [4], we
found three remote structural homologues of BA42. One of these homologues was
recently characterized as an acid phosphatase of the thylakoid lumen in plants
[5]. We will present the first biochemical evidences showing that BA42 presents
phosphatase activity as well, pointing to the discovery of a novel type of
phosphatases associated to the DUF477 domain.