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New page: left|200px<br /><applet load="1cq5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cq5" /> '''NMR STRUCTURE OF SRP RNA DOMAIN IV'''<br /> ... |
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== | ==NMR STRUCTURE OF SRP RNA DOMAIN IV== | ||
The signal recognition particle (SRP) is a phylogenetically conserved | <StructureSection load='1cq5' size='340' side='right'caption='[[1cq5]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1cq5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CQ5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cq5 OCA], [https://pdbe.org/1cq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cq5 RCSB], [https://www.ebi.ac.uk/pdbsum/1cq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cq5 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The signal recognition particle (SRP) is a phylogenetically conserved ribonucleoprotein required for cotranslational targeting of proteins to the membrane of the endoplasmic reticulum of the bacterial plasma membrane. Domain IV of SRP RNA consists of a short stem-loop structure with two internal loops that contain the most conserved nucleotides of the molecule. All known essential interactions of SRP occur in that moiety containing domain IV. The solution structure of a 43-nt RNA comprising the complete Escherichia coli domain IV was determined by multidimensional NMR and restrained molecular dynamics refinement. Our data confirm the previously determined rigid structure of a smaller subfragment containing the most conserved, symmetric internal loop A (Schmitz et al., Nat Struct Biol, 1999, 6:634-638), where all conserved nucleotides are involved in nucleotide-specific structural interactions. Asymmetric internal loop B provides a hinge in the RNA molecule; it is partially flexible, yet also uniquely structured. The longer strand of internal loop B extends the major groove by creating a ledge-like arrangement; for loop B however, there is no obvious structural role for the conserved nucleotides. The structure of domain IV suggests that loop A is the initial site for the RNA/protein interaction creating specificity, whereas loop B provides a secondary interaction site. | |||
Structure of the phylogenetically most conserved domain of SRP RNA.,Schmitz U, Behrens S, Freymann DM, Keenan RJ, Lukavsky P, Walter P, James TL RNA. 1999 Nov;5(11):1419-29. PMID:10580470<ref>PMID:10580470</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1cq5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Behrens | [[Category: Behrens S]] | ||
[[Category: Freymann | [[Category: Freymann DM]] | ||
[[Category: James | [[Category: James TL]] | ||
[[Category: Lukavsky | [[Category: Lukavsky P]] | ||
[[Category: Schmitz | [[Category: Schmitz U]] | ||
[[Category: Walter | [[Category: Walter P]] | ||
Latest revision as of 14:39, 22 November 2023
NMR STRUCTURE OF SRP RNA DOMAIN IVNMR STRUCTURE OF SRP RNA DOMAIN IV
Structural highlights
Publication Abstract from PubMedThe signal recognition particle (SRP) is a phylogenetically conserved ribonucleoprotein required for cotranslational targeting of proteins to the membrane of the endoplasmic reticulum of the bacterial plasma membrane. Domain IV of SRP RNA consists of a short stem-loop structure with two internal loops that contain the most conserved nucleotides of the molecule. All known essential interactions of SRP occur in that moiety containing domain IV. The solution structure of a 43-nt RNA comprising the complete Escherichia coli domain IV was determined by multidimensional NMR and restrained molecular dynamics refinement. Our data confirm the previously determined rigid structure of a smaller subfragment containing the most conserved, symmetric internal loop A (Schmitz et al., Nat Struct Biol, 1999, 6:634-638), where all conserved nucleotides are involved in nucleotide-specific structural interactions. Asymmetric internal loop B provides a hinge in the RNA molecule; it is partially flexible, yet also uniquely structured. The longer strand of internal loop B extends the major groove by creating a ledge-like arrangement; for loop B however, there is no obvious structural role for the conserved nucleotides. The structure of domain IV suggests that loop A is the initial site for the RNA/protein interaction creating specificity, whereas loop B provides a secondary interaction site. Structure of the phylogenetically most conserved domain of SRP RNA.,Schmitz U, Behrens S, Freymann DM, Keenan RJ, Lukavsky P, Walter P, James TL RNA. 1999 Nov;5(11):1419-29. PMID:10580470[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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