TY - JOUR
T1 - Structure of a symmetric photosynthetic reaction center-photosystem
AU - Gisriel, Christopher
AU - Sarrou, Iosifina
AU - Ferlez, Bryan
AU - Golbeck, John H.
AU - Redding, Kevin
AU - Fromme, Raimund
N1 - Funding Information:
We are grateful to J. Whitelegge for his validation of the PshX sequence by mass spectrometry and to Y. Mazor for modeling and graphical assistance. This work was funded by the Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences, of the U.S. Department of Energy (DOE) through grant DE-SC0010575 to K.E.R., R.F., and J.H.G. and supported with x-ray crystallographic equipment and infrastructure provided by P. Fromme of the Biodesign Center for Applied Structural Discovery at Arizona State University. The Berkeley Center for Structural Biology is supported in part by the National Institutes of Health, National Institute of General Medical Sciences, and the Howard Hughes Medical Institute. The Advanced Light Source is a DOE Scientific User Facility supported by the Director, Office of Science, Office of Basic Energy Sciences and operated for the DOE Office of Science by Lawrence Berkeley National Laboratory. Results shown in this report are derived from work performed at Argonne National Laboratory, Structural Biology Center at the Advanced Photon Source. The Structural Biology Center is funded by the DOE Office of Science, Office of Biological and Environmental Research. Argonne is operated by UChicago Argonne, LLC, for the DOE Office of Science under contract DE-AC02-06CH11357. K.E.R., J.H.G., and R.F. designed the project. I.S. and C.G. performed purifications, their subsequent optimization, and characterization. C.G., B.F., and R.F. optimized crystallization conditions. C.G. crystallized HbRC that was used in x-ray diffraction experiments. R.F. and C.G. collected x-ray diffraction data. R.F. and C.G. built models for molecular replacement phasing of diffraction data. R.F. and C.G. performed model building and refinement. C.G., K.E.R., and R.F. wrote the manuscript with input from all other authors. The HbRC structure has been deposited into the Protein Data Bank with accession code 5V8K. The authors declare no competing financial interests.
PY - 2017/9/8
Y1 - 2017/9/8
N2 - Reaction centers are pigment-protein complexes that drive photosynthesis by converting light into chemical energy. It is believed that they arose once froma homodimeric protein. The symmetry of a homodimer is broken in heterodimeric reaction-center structures, such as those reported previously. The 2.2-angstrom resolution x-ray structure of the homodimeric reaction center-photosystem from the phototroph Heliobacterium modesticaldum exhibits perfect C2 symmetry. The core polypeptide dimer and two small subunits coordinate 54 bacteriochlorophylls and 2 carotenoids that capture and transfer energy to the electron transfer chain at the center, which performs charge separation and consists of 6 (bacterio)chlorophylls and an iron-sulfur cluster; unlike other reaction centers, it lacks a bound quinone. This structure preserves characteristics of the ancestral reaction center, providing insight into the evolution of photosynthesis.
AB - Reaction centers are pigment-protein complexes that drive photosynthesis by converting light into chemical energy. It is believed that they arose once froma homodimeric protein. The symmetry of a homodimer is broken in heterodimeric reaction-center structures, such as those reported previously. The 2.2-angstrom resolution x-ray structure of the homodimeric reaction center-photosystem from the phototroph Heliobacterium modesticaldum exhibits perfect C2 symmetry. The core polypeptide dimer and two small subunits coordinate 54 bacteriochlorophylls and 2 carotenoids that capture and transfer energy to the electron transfer chain at the center, which performs charge separation and consists of 6 (bacterio)chlorophylls and an iron-sulfur cluster; unlike other reaction centers, it lacks a bound quinone. This structure preserves characteristics of the ancestral reaction center, providing insight into the evolution of photosynthesis.
UR - http://www.scopus.com/inward/record.url?scp=85026489823&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85026489823&partnerID=8YFLogxK
U2 - 10.1126/science.aan5611
DO - 10.1126/science.aan5611
M3 - Article
C2 - 28751471
AN - SCOPUS:85026489823
SN - 0036-8075
VL - 357
SP - 1021
EP - 1025
JO - Science
JF - Science
IS - 6355
ER -