6FRK

Structure of a prehandover mammalian ribosomal SRP and SRP receptor targeting complex

This is a non-PDB format compatible entry.

Summary for 6FRK

• Entry DOI: 10.2210/pdb6frk/pdb
• EMDB information: 4300
• Descriptor: Canis lupus familiaris RNA, 7SL, cytoplasmic 1 (RN7SL1), SRP RNA, Ribosomal protein uL3, Ribosomal protein uL4, ... (62 entities in total)
• Functional Keywords: er membrane targeting ribosome signal recognition particle, translation
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Cytoplasm : Q00004 P21262 P61010 P16255
• Total number of polymer chains: 58
• Total formula weight: 2504827.71

Authors

Kobayashi, K.,Jomaa, A.,Ban, N. (deposition date: 2018-02-16, release date: 2018-03-28, Last modification date: 2018-05-02)

Primary citation

Kobayashi, K.,Jomaa, A.,Lee, J.H.,Chandrasekar, S.,Boehringer, D.,Shan, S.O.,Ban, N.
Structure of a prehandover mammalian ribosomal SRP·SRP receptor targeting complex.
Science, 360:323-327, 2018

PubMed Abstract: Signal recognition particle (SRP) targets proteins to the endoplasmic reticulum (ER). SRP recognizes the ribosome synthesizing a signal sequence and delivers it to the SRP receptor (SR) on the ER membrane followed by the transfer of the signal sequence to the translocon. Here, we present the cryo-electron microscopy structure of the mammalian translating ribosome in complex with SRP and SR in a conformation preceding signal sequence handover. The structure visualizes all eukaryotic-specific SRP and SR proteins and reveals their roles in stabilizing this conformation by forming a large protein assembly at the distal site of SRP RNA. We provide biochemical evidence that the guanosine triphosphate hydrolysis of SRP·SR is delayed at this stage, possibly to provide a time window for signal sequence handover to the translocon.

PubMed: 29567807
DOI: 10.1126/science.aar7924

Experimental method

ELECTRON MICROSCOPY (3.7 Å)