TY - JOUR
T1 - Changes in non-core regions stabilise plastocyanin from the thermophilic cyanobacterium Phormidium laminosum
AU - Muñoz-López, Francisco J.
AU - Raugei, Simone
AU - De La Rosa, Miguel A.
AU - Díaz-Quintana, Antonio J.
AU - Carloni, Paolo
N1 - Funding Information:
Acknowledgments The authors thank J. Angulo for critical reading of the manuscript. This work was supported by research grants from the Spanish Ministry of Science and Innovation (BFU2006-01361), the Andalusian Government (BIO-198 and P06-CVI-01713) and Project HPC-EUROPA?? (RII3-CT-2003-506079), with the support of the European Union Research Infrastructure Action under the Sixth Frame Programme ‘‘Structuring the European Research Area’’ programme. F.J.M.-L. is the recipient of an FPI fellowship (BES-2005-10404) from the Spanish Ministry of Science and Innovation.
PY - 2010/3
Y1 - 2010/3
N2 - We report a theoretical investigation on the different stabilities of two plastocyanins. The first one belongs to the thermophilic cyanobacterium Phormidium laminosum and the second one belongs to its mesophilic relative Synechocystis sp. These proteins share the same topology and secondary-structure elements; however, the melting temperatures of their oxidised species differ by approximately 15 K. Long-time-scale molecular dynamics simulations, performed at different temperatures, show that the thermophilic protein optimises a set of intramolecular interactions (interstrand hydrogen bonding, salt bridging and hydrophobic clustering) within the region that comprises the strands β5 and β6, loop L5 and the helix. This region exhibits most of the differences in the primary sequence between the two proteins and, in addition, it is involved in the interaction with known physiological partners. Further work is in progress to unveil the specific structural features responsible for the different thermal stability of the two proteins.
AB - We report a theoretical investigation on the different stabilities of two plastocyanins. The first one belongs to the thermophilic cyanobacterium Phormidium laminosum and the second one belongs to its mesophilic relative Synechocystis sp. These proteins share the same topology and secondary-structure elements; however, the melting temperatures of their oxidised species differ by approximately 15 K. Long-time-scale molecular dynamics simulations, performed at different temperatures, show that the thermophilic protein optimises a set of intramolecular interactions (interstrand hydrogen bonding, salt bridging and hydrophobic clustering) within the region that comprises the strands β5 and β6, loop L5 and the helix. This region exhibits most of the differences in the primary sequence between the two proteins and, in addition, it is involved in the interaction with known physiological partners. Further work is in progress to unveil the specific structural features responsible for the different thermal stability of the two proteins.
KW - Blue copper protein
KW - Molecular dynamics
KW - Plastocyanin
KW - Protein stability
KW - Thermophilic cyanobacteria
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U2 - 10.1007/s00775-009-0605-6
DO - 10.1007/s00775-009-0605-6
M3 - Article
C2 - 19915878
AN - SCOPUS:77949261588
VL - 15
SP - 329
EP - 338
JO - Journal of Biological Inorganic Chemistry
JF - Journal of Biological Inorganic Chemistry
SN - 0949-8257
IS - 3
ER -