High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium Export

@article{citeulike:4277556, abstract = {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 over-all 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 of tRNA.}, author = {Harms, Joerg and Schluenzen, Frank and Zarivach, Raz and Bashan, Anat and Gat, Sharon and Agmon, Ilana and Bartels, Heike and Franceschi, Fran\c{c}ois and Yonath, Ada}, citeulike-article-id = {4277556}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0092-8674(01)00546-3}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0092867401005463}, day = {30}, doi = {10.1016/S0092-8674(01)00546-3}, issn = {00928674}, journal = {Cell}, keywords = {experiment, protein, ribosome, rna, structure, xray-crystal-structure}, month = {November}, number = {5}, pages = {679--688}, posted-at = {2009-04-06 08:51:19}, priority = {2}, title = {High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium}, url = {http://dx.doi.org/10.1016/S0092-8674(01)00546-3}, volume = {107}, year = {2001} }

TY - JOUR ID - citeulike:4277556 L3 - citeulike-article-id:4277556 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 over-all 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 of tRNA. IS - 5 JF - Cell SN - 00928674 EP - 688 TI - High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium VL - 107 SP - 679 KW - experiment KW - protein KW - ribosome KW - rna KW - structure KW - xray-crystal-structure 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 PY - 2001/11/30/ UR - http://dx.doi.org/10.1016/S0092-8674(01)00546-3 ER -