FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1990731282> ?p ?o ?g. }

• W1990731282 abstract "Introduction Initiation of protein synthesis is a key step in the control of gene expression. In eukaryotes, initiation is a highly complex process that requires almost a dozen protein factors. The last step involves joining of the large and small subunits of the ribosome to form the 80 S initiation complex with the transfer RNA (tRNA) in the P-site base paired to the start codon. This step is catalyzed by the guanosine triphosphatase (GTPase) factor eIF5B. In addition, eIF5B is thought to play a role in ensuring that translation initiation takes place only on mature ribosomes. Methods The development of fast, direct electron detectors and new methods of image analysis for cryo–electron microscopy allow high-resolution reconstructions from much smaller numbers of particles than previously possible. We used these new methods to provide feedback to improve the biochemical preparation of samples for structure determination of the eukaryotic translation initiation complex with initiator tRNA and eIF5B, which was trapped on the ribosome with the nonhydrolyzable GTP analog GDPCP. Results Although the structure of the fully assembled complex was calculated from only 5143 particles, representing just 3% of the population in the sample, it was possible to obtain a resolution of 6.6 Å. This allowed us to propose a molecular model for the initiation complex. The structure shows that the subunits of the ribosome are rotated relative to the canonical state after initiation. The long helix and C-terminal domain of eIF5B have changed conformation and moved into the ribosome, where the C-terminal domain interacts with the initiator tRNA. The tRNA is stabilized in a distorted conformation, with its 3′-CCA end out of the peptidyl transferase center. Discussion The conformational change in eIF5B may be induced upon binding to the small (40 S ) subunit when it specifically recognizes initiator tRNA. In its altered conformation, eIF5B interacts simultaneously with the initiator tRNA and the GTPase center of the ribosome, thus coupling GTP hydrolysis with tRNA recognition in the ribosome. The large number of contacts made by eIF5B with the ribosomal subunits and tRNA is consistent with its role in subunit joining. A close contact with the eukaryote-specific ribosomal protein L40 would not be possible in the immature ubiquitinated form of L40, thus precluding the recruitment of immature 60 S subunits. A comparison with previous work on the bacterial homolog IF2 suggests that the mechanism of this step of initiation is conserved across kingdoms. Finally, the use of recent advances in cryo-EM to determine a relatively high-resolution structure of the eIF5B-ribosome complex from a very small fraction of a sample could be a general approach for the study of other dynamic or transient biological complexes." @default.
• W1990731282 created "2016-06-24" @default.
• W1990731282 creator A5014221058 @default.
• W1990731282 creator A5059939534 @default.
• W1990731282 creator A5061614353 @default.
• W1990731282 creator A5062177977 @default.
• W1990731282 creator A5073767436 @default.
• W1990731282 creator A5082458083 @default.
• W1990731282 creator A5086176987 @default.
• W1990731282 date "2013-11-15" @default.
• W1990731282 modified "2023-09-27" @default.
• W1990731282 title "Molecular Architecture of a Eukaryotic Translational Initiation Complex" @default.
• W1990731282 cites W1493552793 @default.
• W1990731282 cites W1554349566 @default.
• W1990731282 cites W174730266 @default.
• W1990731282 cites W1966992478 @default.
• W1990731282 cites W1971090312 @default.
• W1990731282 cites W1978870437 @default.
• W1990731282 cites W1985441949 @default.
• W1990731282 cites W2008410413 @default.
• W1990731282 cites W2011665065 @default.
• W1990731282 cites W2024684906 @default.
• W1990731282 cites W2025595745 @default.
• W1990731282 cites W2037313242 @default.
• W1990731282 cites W2044553149 @default.
• W1990731282 cites W2048558269 @default.
• W1990731282 cites W2050656609 @default.
• W1990731282 cites W2060167034 @default.
• W1990731282 cites W2073949924 @default.
• W1990731282 cites W2075268529 @default.
• W1990731282 cites W2075554307 @default.
• W1990731282 cites W2075824676 @default.
• W1990731282 cites W2080190754 @default.
• W1990731282 cites W2081540493 @default.
• W1990731282 cites W2081545937 @default.
• W1990731282 cites W2089238459 @default.
• W1990731282 cites W2100455255 @default.
• W1990731282 cites W2104234755 @default.
• W1990731282 cites W2105460881 @default.
• W1990731282 cites W2121596680 @default.
• W1990731282 cites W2124026197 @default.
• W1990731282 cites W2131021422 @default.
• W1990731282 cites W2132629607 @default.
• W1990731282 cites W2133932548 @default.
• W1990731282 cites W2139519590 @default.
• W1990731282 cites W2142111672 @default.
• W1990731282 cites W2152425069 @default.
• W1990731282 cites W2152562710 @default.
• W1990731282 cites W2160559764 @default.
• W1990731282 cites W2165048399 @default.
• W1990731282 cites W2916336743 @default.
• W1990731282 doi "https://doi.org/10.1126/science.1240585" @default.
• W1990731282 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3836175" @default.
• W1990731282 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24200810" @default.
• W1990731282 hasPublicationYear "2013" @default.
• W1990731282 type Work @default.
• W1990731282 sameAs 1990731282 @default.
• W1990731282 citedByCount "122" @default.
• W1990731282 countsByYear W19907312822014 @default.
• W1990731282 countsByYear W19907312822015 @default.
• W1990731282 countsByYear W19907312822016 @default.
• W1990731282 countsByYear W19907312822017 @default.
• W1990731282 countsByYear W19907312822018 @default.
• W1990731282 countsByYear W19907312822019 @default.
• W1990731282 countsByYear W19907312822020 @default.
• W1990731282 countsByYear W19907312822021 @default.
• W1990731282 countsByYear W19907312822022 @default.
• W1990731282 countsByYear W19907312822023 @default.
• W1990731282 crossrefType "journal-article" @default.
• W1990731282 hasAuthorship W1990731282A5014221058 @default.
• W1990731282 hasAuthorship W1990731282A5059939534 @default.
• W1990731282 hasAuthorship W1990731282A5061614353 @default.
• W1990731282 hasAuthorship W1990731282A5062177977 @default.
• W1990731282 hasAuthorship W1990731282A5073767436 @default.
• W1990731282 hasAuthorship W1990731282A5082458083 @default.
• W1990731282 hasAuthorship W1990731282A5086176987 @default.
• W1990731282 hasBestOaLocation W19907312821 @default.
• W1990731282 hasConcept C104317684 @default.
• W1990731282 hasConcept C105580179 @default.
• W1990731282 hasConcept C12554922 @default.
• W1990731282 hasConcept C129194359 @default.
• W1990731282 hasConcept C149364088 @default.
• W1990731282 hasConcept C153957851 @default.
• W1990731282 hasConcept C176990463 @default.
• W1990731282 hasConcept C185592680 @default.
• W1990731282 hasConcept C207332259 @default.
• W1990731282 hasConcept C3675279 @default.
• W1990731282 hasConcept C4718897 @default.
• W1990731282 hasConcept C55493867 @default.
• W1990731282 hasConcept C62493599 @default.
• W1990731282 hasConcept C67705224 @default.
• W1990731282 hasConcept C77430603 @default.
• W1990731282 hasConcept C8010536 @default.
• W1990731282 hasConcept C86803240 @default.
• W1990731282 hasConcept C88478588 @default.
• W1990731282 hasConcept C95444343 @default.
• W1990731282 hasConcept C97154109 @default.
• W1990731282 hasConcept C99348085 @default.
• W1990731282 hasConceptScore W1990731282C104317684 @default.
• W1990731282 hasConceptScore W1990731282C105580179 @default.

• next