TY - JOUR
T1 - High resolution structure of the large ribosomal subunit from a mesophilic eubacterium
AU - Harms, Joerg
AU - Schluenzen, Frank
AU - Zarivach, Raz
AU - Bashan, Anat
AU - Gat, Sharon
AU - Agmon, Ilana
AU - Bartels, Heike
AU - Franceschi, François
AU - Yonath, Ada
N1 - Funding Information:
We thank J.M. Lehn for indispensable advice; M. Pope for the tungsten clusters; M. Wilchek, W. Traub, A. Mankin, and A. Tocilj for critical discussions; R. Wimmer for indicating the ribosome source; R.Albrecht, T. Auerbach, W.S. Bennett, Z. Biron, H. Burmeister, C. Brune, C. Glotz, M. Gluehmann, G. Goeltz, H.A.S. Hansen, M. Kessler, M. Laschever, S. Meier, J. Muessig, M. Peretz, M. Pioletti, C. Radzwill, B. Schmidt, and A. Wieweger for contributing to different stages of the research. These studies could not be performed without the cooperation of the staff of the synchrotron radiation facilities at EMBL and MPG at DESY; ID14/2 and 4 at EMBL/ESRF, and ID19/APS/ANL. Support was provided by the Max-Planck Society, the U.S. National Institutes of Health (GM34360), the German Ministry for Science and Technology (grant 05-641EA), and the Kimmelman Center for Macromolecular Assembly at the Weizmann Institute. A.Y. holds the Martin S. Kimmel Professorial Chair.
PY - 2001/11/30
Y1 - 2001/11/30
N2 - We describe the high resolution structure of the large ribosomal subunit from Deinococcus radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and functionally relevant ligands. The overall structure of D50S is similar to that from the archae bacterium Haloarcula marismortui (H50S); however, a detailed comparison revealed significant differences, for example, in the orientation of nucleotides in peptidyl transferase center and in the structures of many ribosomal proteins. Analysis of ribosomal features involved in dynamic aspects of protein biosynthesis that are partially or fully disordered in H50S revealed the conformations of intersubunit bridges in unbound subunits, suggesting how they may change upon subunit association and how movements of the L1-stalk may facilitate the exit tRNA.
AB - We describe the high resolution structure of the large ribosomal subunit from Deinococcus radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and functionally relevant ligands. The overall structure of D50S is similar to that from the archae bacterium Haloarcula marismortui (H50S); however, a detailed comparison revealed significant differences, for example, in the orientation of nucleotides in peptidyl transferase center and in the structures of many ribosomal proteins. Analysis of ribosomal features involved in dynamic aspects of protein biosynthesis that are partially or fully disordered in H50S revealed the conformations of intersubunit bridges in unbound subunits, suggesting how they may change upon subunit association and how movements of the L1-stalk may facilitate the exit tRNA.
UR - http://www.scopus.com/inward/record.url?scp=0035977093&partnerID=8YFLogxK
U2 - 10.1016/S0092-8674(01)00546-3
DO - 10.1016/S0092-8674(01)00546-3
M3 - Article
AN - SCOPUS:0035977093
SN - 0092-8674
VL - 107
SP - 679
EP - 688
JO - Cell
JF - Cell
IS - 5
ER -