FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2039258652> ?p ?o ?g. }

• W2039258652 endingPage "912" @default.
• W2039258652 startingPage "901" @default.
• W2039258652 abstract "Abstract High‐resolution structures of both ribosomal subunits revealed that most stages of protein biosynthesis, including decoding of genetic information, are navigated and controlled by the elaborate ribosomal architectural‐design. Remote interactions govern accurate substrate alignment within a flexible active‐site pocket [peptidyl transferase center (PTC)], and spatial considerations, due mainly to a universal mobile nucleotide, U2585, ensure proper chirality by interfering with D ‐amino‐acids incorporation. tRNA translocation involves two correlated motions: overall mRNA/tRNA (messenger and transfer RNA) shift, and a rotation of the tRNA single‐stranded aminoacylated‐3′ end around the bond connecting it with the tRNA helical‐regions. This bond coincides with an axis passing through a sizable symmetry‐related region, identified around the PTC in all large‐subunit crystal structures. Propelled by a bulged universal nucleotide, A2602, positioned at the two‐fold symmetry axis, and guided by a ribosomal‐RNA scaffold along an exact pattern, the rotatory motion results in stereochemistry optimal for peptide‐bond formation and in geometry ensuring nascent proteins entrance into their exit tunnel. Hence, confirming that ribosomes contribute positional rather than chemical catalysis, and that peptide bond formation is concurrent with A‐ to P‐site tRNA passage. Connecting between the PTC, the decoding center, the tRNA entrance and exit points, the symmetry‐related region can transfer intra‐ribosomal signals between remote functional locations, guaranteeing smooth processivity of amino acids polymerization. Ribosomal proteins are involved in accurate substrate placement (L16), discrimination and signal transmission (L22) and protein biosynthesis regulation (CTC). Residing on the exit tunnel walls near its entrance, and stretching to its opening, protein‐L22 can mediate ribosome response to cellular regulatory signals, since it can swing across the tunnel, causing gating and elongation arrest. Each of the protein CTC domains has a defined task. The N ‐terminal domain stabilizes the intersubunit‐bridge confining the A‐site‐tRNA entrance. The middle domain protects the bridge conformation at elevated temperatures. The C ‐terminal domain can undergo substantial conformational rearrangements upon substrate binding, indicating CTC participation in biosynthesis‐control under stressful conditions. Copyright © 2004 John Wiley & Sons, Ltd." @default.
• W2039258652 created "2016-06-24" @default.
• W2039258652 creator A5001676407 @default.
• W2039258652 creator A5006229060 @default.
• W2039258652 creator A5010344878 @default.
• W2039258652 creator A5016847667 @default.
• W2039258652 creator A5020190688 @default.
• W2039258652 creator A5022351039 @default.
• W2039258652 creator A5028565143 @default.
• W2039258652 creator A5046434797 @default.
• W2039258652 creator A5046561508 @default.
• W2039258652 creator A5055375647 @default.
• W2039258652 creator A5057082623 @default.
• W2039258652 creator A5058026766 @default.
• W2039258652 creator A5063042386 @default.
• W2039258652 creator A5075304102 @default.
• W2039258652 creator A5080786712 @default.
• W2039258652 creator A5080908408 @default.
• W2039258652 creator A5091222597 @default.
• W2039258652 date "2004-08-31" @default.
• W2039258652 modified "2023-10-16" @default.
• W2039258652 title "Functional aspects of ribosomal architecture: symmetry, chirality and regulation" @default.
• W2039258652 cites W1484216450 @default.
• W2039258652 cites W1485797794 @default.
• W2039258652 cites W1532382519 @default.
• W2039258652 cites W1559844620 @default.
• W2039258652 cites W1653006923 @default.
• W2039258652 cites W1975455557 @default.
• W2039258652 cites W1977287926 @default.
• W2039258652 cites W1983534198 @default.
• W2039258652 cites W1985844054 @default.
• W2039258652 cites W1988858733 @default.
• W2039258652 cites W1995418797 @default.
• W2039258652 cites W1996592126 @default.
• W2039258652 cites W1998564815 @default.
• W2039258652 cites W1999282565 @default.
• W2039258652 cites W1999362400 @default.
• W2039258652 cites W2002532175 @default.
• W2039258652 cites W2008025258 @default.
• W2039258652 cites W2013303604 @default.
• W2039258652 cites W2017372245 @default.
• W2039258652 cites W2018530089 @default.
• W2039258652 cites W2023864622 @default.
• W2039258652 cites W2027195993 @default.
• W2039258652 cites W2027876761 @default.
• W2039258652 cites W2033078843 @default.
• W2039258652 cites W2039846261 @default.
• W2039258652 cites W2039951296 @default.
• W2039258652 cites W2044128661 @default.
• W2039258652 cites W2046938811 @default.
• W2039258652 cites W2049504572 @default.
• W2039258652 cites W2051164564 @default.
• W2039258652 cites W2052668373 @default.
• W2039258652 cites W2053921694 @default.
• W2039258652 cites W2060967348 @default.
• W2039258652 cites W2061146689 @default.
• W2039258652 cites W2063029946 @default.
• W2039258652 cites W2071804506 @default.
• W2039258652 cites W2071840045 @default.
• W2039258652 cites W2077480952 @default.
• W2039258652 cites W2085536565 @default.
• W2039258652 cites W2087679230 @default.
• W2039258652 cites W2088175720 @default.
• W2039258652 cites W2089457247 @default.
• W2039258652 cites W2091797050 @default.
• W2039258652 cites W2092617311 @default.
• W2039258652 cites W2093471887 @default.
• W2039258652 cites W2097654784 @default.
• W2039258652 cites W2098772291 @default.
• W2039258652 cites W2101114936 @default.
• W2039258652 cites W2105289202 @default.
• W2039258652 cites W2110557219 @default.
• W2039258652 cites W2110821985 @default.
• W2039258652 cites W2113761741 @default.
• W2039258652 cites W2119966574 @default.
• W2039258652 cites W2122964499 @default.
• W2039258652 cites W2124433456 @default.
• W2039258652 cites W2133678661 @default.
• W2039258652 cites W2134817259 @default.
• W2039258652 cites W2148198051 @default.
• W2039258652 cites W2149548739 @default.
• W2039258652 cites W2149738995 @default.
• W2039258652 cites W2160552813 @default.
• W2039258652 cites W2160611272 @default.
• W2039258652 cites W2162479002 @default.
• W2039258652 cites W2163313560 @default.
• W2039258652 cites W2166117980 @default.
• W2039258652 cites W2171977674 @default.
• W2039258652 cites W2193266704 @default.
• W2039258652 doi "https://doi.org/10.1002/poc.831" @default.
• W2039258652 hasPublicationYear "2004" @default.
• W2039258652 type Work @default.
• W2039258652 sameAs 2039258652 @default.
• W2039258652 citedByCount "33" @default.
• W2039258652 countsByYear W20392586522012 @default.
• W2039258652 countsByYear W20392586522015 @default.
• W2039258652 countsByYear W20392586522016 @default.
• W2039258652 countsByYear W20392586522017 @default.

• next