INVESTIGADORES
MORENO Silvia Margarita
congresos y reuniones científicas
Título:
INSIGHTS INTO THE STRUCTURE OF BCY1, THE REGULATORY SUBUNIT OF PKA FROM Saccharomyces cerevisiae
Autor/es:
FERNANDEZ NUÑEZ, LUCAS; GONZALEZ BARDECI NICOLAS; BLUMENTHAL DONALD; TURJANSKI ADRIAN; ROSSI SILVIA; MORENO SILVIA
Lugar:
Potrero de los Funes- San Luis
Reunión:
Congreso; 47 Reunion Anual de la SAIB; 2011
Resumen:
Yeast is the first non-metazoan organism for which some structural
information of PKA is available. Our group has obtained the crystal
structure of the cAMP binding domains of Bcy1, the regulatory
subunit of PKA. We now show results that contribute to understand
the structure of the whole Bcy1 dimer. The solution structure of
D140-Bcy1, as well as of whole Bcy1 have been solved by SAXS
(small angle X-ray scattering). The R and D of the two structures g max
(small angle X-ray scattering). The R and D of the two structures g max
140-Bcy1, as well as of whole Bcy1 have been solved by SAXS
(small angle X-ray scattering). The R and D of the two structures g maxg max
were determined. The structure of D140-Bcy1 was modeled ab
initio by using de DAMMIN program. The resulting structure
compares very favorably with the crystal structure, thus confirming
the particular relative orientation of A and B cAMP domains. The
structure of whole Bcy1 seems to be more compact than the one of
RI and RII. The amino termini of R subunits constitute the so called
D/D domain, responsible for the dimerization of the subunits and
for the interaction with anchoring proteins (AKAPs). Chemical
crosslinking experiments confirm that Bcy1 exists as a dimer, via its
N-terminus. The N terminus of Bcy1 was modeled by homology
using Swiss Model and further minimization with GROMACS. The
preliminary model shows that Bcy1 shares with its counterparts the
residues important for dimerization; however the exposed surface,
that should interact with anchoring proteins (not described yet in
yeast) have characteristics of its own.
compares very favorably with the crystal structure, thus confirming
the particular relative orientation of A and B cAMP domains. The
structure of whole Bcy1 seems to be more compact than the one of
RI and RII. The amino termini of R subunits constitute the so called
D/D domain, responsible for the dimerization of the subunits and
for the interaction with anchoring proteins (AKAPs). Chemical
crosslinking experiments confirm that Bcy1 exists as a dimer, via its
N-terminus. The N terminus of Bcy1 was modeled by homology
using Swiss Model and further minimization with GROMACS. The
preliminary model shows that Bcy1 shares with its counterparts the
residues important for dimerization; however the exposed surface,
that should interact with anchoring proteins (not described yet in
yeast) have characteristics of its own.
initio by using de DAMMIN program. The resulting structure
compares very favorably with the crystal structure, thus confirming
the particular relative orientation of A and B cAMP domains. The
structure of whole Bcy1 seems to be more compact than the one of
RI and RII. The amino termini of R subunits constitute the so called
D/D domain, responsible for the dimerization of the subunits and
for the interaction with anchoring proteins (AKAPs). Chemical
crosslinking experiments confirm that Bcy1 exists as a dimer, via its
N-terminus. The N terminus of Bcy1 was modeled by homology
using Swiss Model and further minimization with GROMACS. The
preliminary model shows that Bcy1 shares with its counterparts the
residues important for dimerization; however the exposed surface,
that should interact with anchoring proteins (not described yet in
yeast) have characteristics of its own.
compares very favorably with the crystal structure, thus confirming
the particular relative orientation of A and B cAMP domains. The
structure of whole Bcy1 seems to be more compact than the one of
RI and RII. The amino termini of R subunits constitute the so called
D/D domain, responsible for the dimerization of the subunits and
for the interaction with anchoring proteins (AKAPs). Chemical
crosslinking experiments confirm that Bcy1 exists as a dimer, via its
N-terminus. The N terminus of Bcy1 was modeled by homology
using Swiss Model and further minimization with GROMACS. The
preliminary model shows that Bcy1 shares with its counterparts the
residues important for dimerization; however the exposed surface,
that should interact with anchoring proteins (not described yet in
yeast) have characteristics of its own.
D140-Bcy1 was modeled ab
initio by using de DAMMIN program. The resulting structure
compares very favorably with the crystal structure, thus confirming
the particular relative orientation of A and B cAMP domains. The
structure of whole Bcy1 seems to be more compact than the one of
RI and RII. The amino termini of R subunits constitute the so called
D/D domain, responsible for the dimerization of the subunits and
for the interaction with anchoring proteins (AKAPs). Chemical
crosslinking experiments confirm that Bcy1 exists as a dimer, via its
N-terminus. The N terminus of Bcy1 was modeled by homology
using Swiss Model and further minimization with GROMACS. The
preliminary model shows that Bcy1 shares with its counterparts the
residues important for dimerization; however the exposed surface,
that should interact with anchoring proteins (not described yet in
yeast) have characteristics of its own.
compares very favorably with the crystal structure, thus confirming
the particular relative orientation of A and B cAMP domains. The
structure of whole Bcy1 seems to be more compact than the one of
RI and RII. The amino termini of R subunits constitute the so called
D/D domain, responsible for the dimerization of the subunits and
for the interaction with anchoring proteins (AKAPs). Chemical
crosslinking experiments confirm that Bcy1 exists as a dimer, via its
N-terminus. The N terminus of Bcy1 was modeled by homology
using Swiss Model and further minimization with GROMACS. The
preliminary model shows that Bcy1 shares with its counterparts the
residues important for dimerization; however the exposed surface,
that should interact with anchoring proteins (not described yet in
yeast) have characteristics of its own.
by using de DAMMIN program. The resulting structure
compares very favorably with the crystal structure, thus confirming
the particular relative orientation of A and B cAMP domains. The
structure of whole Bcy1 seems to be more compact than the one of
RI and RII. The amino termini of R subunits constitute the so called
D/D domain, responsible for the dimerization of the subunits and
for the interaction with anchoring proteins (AKAPs). Chemical
crosslinking experiments confirm that Bcy1 exists as a dimer, via its
N-terminus. The N terminus of Bcy1 was modeled by homology
using Swiss Model and further minimization with GROMACS. The
preliminary model shows that Bcy1 shares with its counterparts the
residues important for dimerization; however the exposed surface,
that should interact with anchoring proteins (not described yet in
yeast) have characteristics of its own.