Towards the structure of the C-terminal part of the S-layer protein SbsC.
The S-layer protein SbsC from Geobacillus stearothermophilus ATCC 12980 is the most prevalent single protein produced by the bacterium and covers the complete bacterial surface in the form of a two-dimensional crystalline monolayer. In order to elucidate the structural features of the assembly domains, several N-terminally truncated fragments of SbsC have been crystallized. Crystals obtained from recombinant fragments showed anisotropic diffraction to a maximum of 3.5 A resolution using synchrotron radiation. The best diffracting crystals were obtained from rSbsC(755-1099), an unintentional in situ proteolytic degradation product of rSbsC(447-1099). Crystals were obtained in two different space groups, P2(1) and P4(1)2(1)2, and diffracted to 2.6 and 3 A resolution, respectively. Native and heavy-atom derivative data have been collected. The structure of the C-terminal part will yield atomic resolution information for the domains that are crucial for the assembly of the two-dimensional lattice.
Kroutil
Markus
M
Karl-Franzens University, Institute of Molecular Biosciences, Graz, Austria.
Pavkov
Tea
T
Birner-Gruenberger
Ruth
R
Tesarz
Manfred
M
Sleytr
Uwe B
UB
Egelseer
Eva M
EM
Keller
Walter
W
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D001411:Geobacillus stearothermophilus; D008562:Membrane Glycoproteins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D017434:Protein Structure, Tertiary
D001426:Bacterial Proteins; D008562:Membrane Glycoproteins; D010446:Peptide Fragments; C055764:S-layer proteins