5FLX

Mammalian 40S HCV-IRES complex

Summary for 5FLX

• Entry DOI: 10.2210/pdb5flx/pdb
• EMDB information: 3221
• Descriptor: 18S RRNA, 40S RIBOSOMAL PROTEIN S8, 40S RIBOSOMAL PROTEIN S9, ... (37 entities in total)
• Functional Keywords: ribosome, translation initiation, hepatitis c virus internal ribosome entry site
• Biological source: HEPATITIS C VIRUS (HCV); More
• Cellular location: Cytoplasm : P62241 P46781 P46783 P25398 P62269 P60866 P61247 P23396; Cell membrane: P08865; Nucleus : P39019; Ubiquitin: Cytoplasm : P62979; Cell membrane ; Peripheral membrane protein: P63244; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome : P62081
• Total number of polymer chains: 35
• Total formula weight: 1385962.24

Authors

Yamamoto, H.,Collier, M.,Loerke, J.,Ismer, J.,Schmidt, A.,Hilal, T.,Sprink, T.,Yamamoto, K.,Mielke, T.,Burger, J.,Shaikh, T.R.,Dabrowski, M.,Hildebrand, P.W.,Scheerer, P.,Spahn, C.M.T. (deposition date: 2015-10-28, release date: 2015-12-23, Last modification date: 2017-08-30)

Primary citation

Yamamoto, H.,Collier, M.,Loerke, J.,Ismer, J.,Schmidt, A.,Hilal, T.,Sprink, T.,Yamamoto, K.,Mielke, T.,Burger, J.,Shaikh, T.R.,Dabrowski, M.,Hildebrand, P.W.,Scheerer, P.,Spahn, C.M.
Molecular Architecture of the Ribosome-Bound Hepatitis C Virus Internal Ribosomal Entry Site RNA.
Embo J., 34:3042-, 2015

PubMed Abstract: Internal ribosomal entry sites (IRESs) are structured cis-acting RNAs that drive an alternative, cap-independent translation initiation pathway. They are used by many viruses to hijack the translational machinery of the host cell. IRESs facilitate translation initiation by recruiting and actively manipulating the eukaryotic ribosome using only a subset of canonical initiation factor and IRES transacting factors. Here we present cryo-EM reconstructions of the ribosome 80S- and 40S-bound Hepatitis C Virus (HCV) IRES. The presence of four subpopulations for the 80S•HCV IRES complex reveals dynamic conformational modes of the complex. At a global resolution of 3.9 Å for the most stable complex, a derived atomic model reveals a complex fold of the IRES RNA and molecular details of its interaction with the ribosome. The comparison of obtained structures explains how a modular architecture facilitates mRNA loading and tRNA binding to the P-site. This information provides the structural foundation for understanding the mechanism of HCV IRES RNA-driven translation initiation.

PubMed: 26604301
DOI: 10.15252/EMBJ.201592469

Experimental method

ELECTRON MICROSCOPY (3.9 Å)