Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon.
In a designed fusion protein the trimeric domain foldon from bacteriophage T4 fibritin was connected to the C terminus of the collagen model peptide (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the three-stranded collagen triple helix. Crystal structure analysis at 2.6 A resolution revealed conformational changes within the interface of both domains compared with the structure of the isolated molecules. A striking feature is an angle of 62.5 degrees between the symmetry axis of the foldon trimer and the axis of the triple helix. The melting temperature of (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is higher than that of isolated (GlyProPro)(10,) which suggests an entropic stabilization compensating for the destabilization at the interface.
Stetefeld
Jörg
J
Department of Biophysical Chemistry, University of Basel, Klingelbergstrasse 70, CH-4056, Basel, Switzerland. joerg.stetefeld@unibas.ch
Frank
Sabine
S
Jenny
Margrit
M
Schulthess
Therese
T
Kammerer
Richard A
RA
Boudko
Sergei
S
Landwehr
Ruth
R
Okuyama
Kenji
K
Engel
Jürgen
J
D000818:Animals; D003094:Collagen / Q000378:metabolism*; D018360:Crystallography, X-Ray; D006801:Humans; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011108:Polymers; D015202:Protein Engineering; D017434:Protein Structure, Tertiary
D010455:Peptides; D011108:Polymers; C061813:glycine-proline-proline polymer; D003094:Collagen