FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2137085237> ?p ?o ?g. }

• W2137085237 abstract "A novel mechanism for the very first step in polypep-tide elongation on the ribosome has recently been pro-posed by Simonson and Lake (2002)+According to theirtransorientation hypothesis, the incoming aminoacyl-transfer RNA (aa-tRNA) initially binds to the messen-ger RNA (mRNA) with the anticodon stacked on the 59side of the anticodon loop; then, following GTP hydro-lysis, the tRNAswings into theA-site by switching fromthe 59-stacked conformation to the classic 39-stackedgeometry while maintaining Watson–Crick base pair-ing with the mRNA+ There are several serious prob-lems with this proposal+Simonson and Lake inferred the position of theaa-tRNA from immunoelectron microscopy mapping ofthe EF-Tu•GTP•tRNAternary complex on the 30S ribo-somal subunit+ Although this procedure may provide ageneral location for EF-Tu, it is intrinsically incapable ofrevealing the orientation of the incoming tRNA whenthe anticodon first approaches the codon in the 70Sribosome+ Moreover, the binding of the ternary com-plex to the isolated 30S subunit at the A-site in theabsence of the 50S subunit does not occur as part of aphysiological process+ There is, at present, no directexperimental evidence supporting the proposed orien-tation of the EF-Tu•tRNAcomplex at the putative D-sitein the intact ribosome+One major difficulty with the transorientation modelis that it places EF-Tu domain I, which contains theGTPase center, more than 90 A from the a-sarcin-ricin loop (SRL) of the 50S subunit (Fig+ 1)+ TheEF-Tu•GTP•tRNAternarycomplexandEF-Gareknownto have common binding sites on the ribosome, as hasbeen shown by biochemical experiments (Moazed et al+,1988) and by cryo-EM studies (Agrawal et al+, 2000a,2000b)+ These studies have indicated that the GTP-binding domains of both factors lie within5AoftheSRLofthe50Ssubunit+BecausethestructuresofEF-Tuin the cryo-EM study of the kirromycin-stalled 70Sribosome•EF-Tu•GDP•aa-tRNAcomplex(Agrawaletal+,2000a) and the one solved by X-ray crystallography ofthe EF-Tu•GMPPNP•aa-tRNA complex (Nissen et al+,1995) were found to be very similar, and given the factthat kirromycin prevents conformational changes ofEF-Tu immediately after GTP hydrolysis, a large con-formational change between the GTP and GDP statesof the kirromycin-stalled EF-Tu is not expected+ Thetransorientation hypothesis puts EF-Tu in a positionwhere its GTP-binding domain cannot make any con-tact with the SRL (Fig+ 1), even when a very largeconformationalchangeinEF-Tuisallowedtotakeplace+The transorientation model presents serious stericproblems as well+ The authors acknowledge that thereare steric conflicts between EF-Tu and the 50S subunitwhen EF-Tu is docked at the putative D-site+The trans-orientation hypothesis requires L11 and nt 1057–1081of the 23S rRNA to undergo drastic conformationalchanges to permit binding of the ternary complex+Afarsimpler explanation is that EF-Tu binds to the ribosomein the same orientation as seen in cryo-EM reconstruc-tions (Fig+ 1)+ In this orientation, EF-Tu can make con-tact with both L11 and the SRL with no steric conflicts+In transorientation, a steric clash would also occurwhen the aa-tRNA swings from the D-site to the A-site,as it would be forced to sweep through parts of the 50Ssubunit+ In the absence of detailed models for possibleconformational changes in the 50S subunit, it is notpossible to evaluate the claim that transorientation “oc-curs without significant clash +++ between the EF-Tu-" @default.
• W2137085237 created "2016-06-24" @default.
• W2137085237 creator A5021757579 @default.
• W2137085237 creator A5042892654 @default.
• W2137085237 creator A5068698824 @default.
• W2137085237 creator A5076801513 @default.
• W2137085237 creator A5088307660 @default.
• W2137085237 date "2002-09-01" @default.
• W2137085237 modified "2023-09-23" @default.
• W2137085237 title "Problems with the transorientation hypothesis" @default.
• W2137085237 cites W1979048982 @default.
• W2137085237 cites W1979366159 @default.
• W2137085237 cites W2000064612 @default.
• W2137085237 cites W2050329965 @default.
• W2137085237 cites W2058433168 @default.
• W2137085237 cites W2066543062 @default.
• W2137085237 cites W2116458567 @default.
• W2137085237 doi "https://doi.org/10.1017/s1355838202027061" @default.
• W2137085237 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1370322" @default.
• W2137085237 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12358427" @default.
• W2137085237 hasPublicationYear "2002" @default.
• W2137085237 type Work @default.
• W2137085237 sameAs 2137085237 @default.
• W2137085237 citedByCount "4" @default.
• W2137085237 crossrefType "journal-article" @default.
• W2137085237 hasAuthorship W2137085237A5021757579 @default.
• W2137085237 hasAuthorship W2137085237A5042892654 @default.
• W2137085237 hasAuthorship W2137085237A5068698824 @default.
• W2137085237 hasAuthorship W2137085237A5076801513 @default.
• W2137085237 hasAuthorship W2137085237A5088307660 @default.
• W2137085237 hasBestOaLocation W21370852371 @default.
• W2137085237 hasConcept C104292427 @default.
• W2137085237 hasConcept C104317684 @default.
• W2137085237 hasConcept C106774688 @default.
• W2137085237 hasConcept C107824862 @default.
• W2137085237 hasConcept C118716 @default.
• W2137085237 hasConcept C153911025 @default.
• W2137085237 hasConcept C153957851 @default.
• W2137085237 hasConcept C181199279 @default.
• W2137085237 hasConcept C54355233 @default.
• W2137085237 hasConcept C55493867 @default.
• W2137085237 hasConcept C67705224 @default.
• W2137085237 hasConcept C69080955 @default.
• W2137085237 hasConcept C75442077 @default.
• W2137085237 hasConcept C86756495 @default.
• W2137085237 hasConcept C86803240 @default.
• W2137085237 hasConcept C88478588 @default.
• W2137085237 hasConcept C96267730 @default.
• W2137085237 hasConceptScore W2137085237C104292427 @default.
• W2137085237 hasConceptScore W2137085237C104317684 @default.
• W2137085237 hasConceptScore W2137085237C106774688 @default.
• W2137085237 hasConceptScore W2137085237C107824862 @default.
• W2137085237 hasConceptScore W2137085237C118716 @default.
• W2137085237 hasConceptScore W2137085237C153911025 @default.
• W2137085237 hasConceptScore W2137085237C153957851 @default.
• W2137085237 hasConceptScore W2137085237C181199279 @default.
• W2137085237 hasConceptScore W2137085237C54355233 @default.
• W2137085237 hasConceptScore W2137085237C55493867 @default.
• W2137085237 hasConceptScore W2137085237C67705224 @default.
• W2137085237 hasConceptScore W2137085237C69080955 @default.
• W2137085237 hasConceptScore W2137085237C75442077 @default.
• W2137085237 hasConceptScore W2137085237C86756495 @default.
• W2137085237 hasConceptScore W2137085237C86803240 @default.
• W2137085237 hasConceptScore W2137085237C88478588 @default.
• W2137085237 hasConceptScore W2137085237C96267730 @default.
• W2137085237 hasLocation W21370852371 @default.
• W2137085237 hasLocation W21370852372 @default.
• W2137085237 hasLocation W21370852373 @default.
• W2137085237 hasOpenAccess W2137085237 @default.
• W2137085237 hasPrimaryLocation W21370852371 @default.
• W2137085237 hasRelatedWork W141704660 @default.
• W2137085237 hasRelatedWork W1515771519 @default.
• W2137085237 hasRelatedWork W1844278134 @default.
• W2137085237 hasRelatedWork W1903181902 @default.
• W2137085237 hasRelatedWork W1918945878 @default.
• W2137085237 hasRelatedWork W2050521259 @default.
• W2137085237 hasRelatedWork W2063325492 @default.
• W2137085237 hasRelatedWork W2071010926 @default.
• W2137085237 hasRelatedWork W2076281349 @default.
• W2137085237 hasRelatedWork W2080428730 @default.
• W2137085237 hasRelatedWork W2171577342 @default.
• W2137085237 hasRelatedWork W2483171221 @default.
• W2137085237 hasRelatedWork W2758454547 @default.
• W2137085237 hasRelatedWork W2928741147 @default.
• W2137085237 hasRelatedWork W3005144567 @default.
• W2137085237 hasRelatedWork W372883 @default.
• W2137085237 hasRelatedWork W45016482 @default.
• W2137085237 hasRelatedWork W89114292 @default.
• W2137085237 hasRelatedWork W947085050 @default.
• W2137085237 hasRelatedWork W2509242658 @default.
• W2137085237 isParatext "false" @default.
• W2137085237 isRetracted "false" @default.
• W2137085237 magId "2137085237" @default.
• W2137085237 workType "article" @default.