5A9Z

Complex of Thermous thermophilus ribosome bound to BipA-GDPCP

This is a non-PDB format compatible entry.

Summary for 5A9Z

• Entry DOI: 10.2210/pdb5a9z/pdb
• EMDB information: 6396
• Descriptor: 23S ribosomal RNA, 50S ribosomal protein L11, 50S ribosomal protein L13, ... (57 entities in total)
• Functional Keywords: bipa, ribosome, translational gtpase factors, x-ray crystallography and cryo-electron microscopy
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 55
• Total formula weight: 2236387.79

Authors

Kumar, V.,Chen, Y.,Ahmed, T.,Tan, J.,Ero, R.,Bhushan, S.,Gao, Y.-G. (deposition date: 2015-07-23, release date: 2015-10-14, Last modification date: 2024-10-16)

Primary citation

Kumar, V.,Chen, Y.,Ero, R.,Ahmed, T.,Tan, J.,Li, Z.,Wong, A.S.W.,Bhushan, S.,Gao, Y.
Structure of Bipa in GTP Form Bound to the Ratcheted Ribosome.
Proc.Natl.Acad.Sci.USA, 112:10944-10949, 2015

PubMed Abstract: BPI-inducible protein A (BipA) is a member of the family of ribosome-dependent translational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4). Despite being highly conserved in bacteria and playing a critical role in coordinating cellular responses to environmental changes, its structures (isolated and ribosome bound) remain elusive. Here, we present the crystal structures of apo form and GTP analog, GDP, and guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA. In addition to having a distinctive domain arrangement, the C-terminal domain of BipA has a unique fold. Furthermore, we report the cryo-electron microscopy structure of BipA bound to the ribosome in its active GTP form and elucidate the unique structural attributes of BipA interactions with the ribosome and A-site tRNA in the light of its possible function in regulating translation.

PubMed: 26283392
DOI: 10.1073/PNAS.1513216112

Experimental method

ELECTRON MICROSCOPY (4.7 Å)