1SM1

COMPLEX OF THE LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS WITH QUINUPRISTIN AND DALFOPRISTIN

Summary for 1SM1

• Entry DOI: 10.2210/pdb1sm1/pdb
• Related PRD ID: PRD_000505
• Descriptor: 23S RIBOSOMAL RNA, 50S RIBOSOMAL PROTEIN L4, 50S RIBOSOMAL PROTEIN L5, ... (33 entities in total)
• Functional Keywords: ribosome-antibiotic complex, quinupristin, dalfopristin, streptogramins, synercid, ribosome, 50s ribosomal subunit, ribosom-antibiotic complex, ribosome/antibiotic
• Biological source: DEINOCOCCUS RADIODURANS; More
• Total number of polymer chains: 32
• Total formula weight: 1390058.60

Authors

Harms, J.M.,Schluenzen, F.,Fucini, P.,Bartels, H.,Yonath, A. (deposition date: 2004-03-08, release date: 2004-08-03, Last modification date: 2024-07-10)

Primary citation

Harms, J.M.,Schlunzen, F.,Fucini, P.,Bartels, H.,Yonath, A.
Alterations at the Peptidyl Transferase Centre of the Ribosome Induced by the Synergistic Action of the Streptogramins Dalfopristin and Quinupristin.
Bmc Biol., 2:4-, 2004

PubMed Abstract: The bacterial ribosome is a primary target of several classes of antibiotics. Investigation of the structure of the ribosomal subunits in complex with different antibiotics can reveal the mode of inhibition of ribosomal protein synthesis. Analysis of the interactions between antibiotics and the ribosome permits investigation of the specific effect of modifications leading to antimicrobial resistances. Streptogramins are unique among the ribosome-targeting antibiotics because they consist of two components, streptogramins A and B, which act synergistically. Each compound alone exhibits a weak bacteriostatic activity, whereas the combination can act bactericidal. The streptogramins A display a prolonged activity that even persists after removal of the drug. However, the mode of activity of the streptogramins has not yet been fully elucidated, despite a plethora of biochemical and structural data.

PubMed: 15059283
DOI: 10.1186/1741-7007-2-4

Experimental method

X-RAY DIFFRACTION (3.42 Å)