4b5r: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
m Protected "4b5r" [edit=sysop:move=sysop]
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 4b5r is ON HOLD
==SAM-I riboswitch bearing the H. marismortui K-t-7==
<StructureSection load='4b5r' size='340' side='right'caption='[[4b5r]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4b5r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B5R FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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=4b5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b5r OCA], [https://pdbe.org/4b5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b5r RCSB], [https://www.ebi.ac.uk/pdbsum/4b5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b5r ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The k-turn is a widespread structural motif that introduces a tight kink into the helical axis of double-stranded RNA. The adenine bases of consecutive G*A pairs are directed toward the minor groove of the opposing helix, hydrogen bonding in a typical A-minor interaction. We show here that the available structures of k-turns divide into two classes, depending on whether N3 or N1 of the adenine at the 2b position accepts a hydrogen bond from the O2' at the -1n position. There is a coordinated structural change involving a number of hydrogen bonds between the two classes. We show here that Kt-7 can adopt either the N3 or N1 structures depending on environment. While it has the N1 structure in the ribosome, on engineering it into the SAM-I riboswitch, it changes to the N3 structure, resulting in a significant alteration in the trajectory of the helical arms.


Authors: Daldrop, P., Lilley, D.M.J.
The plasticity of a structural motif in RNA: Structural polymorphism of a kink turn as a function of its environment.,Daldrop P, Lilley DM RNA. 2013 Jan 16. PMID:23325110<ref>PMID:23325110</ref>


Description: SAM-I riboswitch bearing the H. marismortui K-t-7
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4b5r" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Riboswitch 3D structures|Riboswitch 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]]
[[Category: Large Structures]]
[[Category: Daldrop P]]
[[Category: Lilley DMJ]]

Latest revision as of 14:43, 20 December 2023

SAM-I riboswitch bearing the H. marismortui K-t-7SAM-I riboswitch bearing the H. marismortui K-t-7

Structural highlights

4b5r is a 1 chain structure with sequence from Caldanaerobacter subterraneus subsp. tengcongensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.95Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

The k-turn is a widespread structural motif that introduces a tight kink into the helical axis of double-stranded RNA. The adenine bases of consecutive G*A pairs are directed toward the minor groove of the opposing helix, hydrogen bonding in a typical A-minor interaction. We show here that the available structures of k-turns divide into two classes, depending on whether N3 or N1 of the adenine at the 2b position accepts a hydrogen bond from the O2' at the -1n position. There is a coordinated structural change involving a number of hydrogen bonds between the two classes. We show here that Kt-7 can adopt either the N3 or N1 structures depending on environment. While it has the N1 structure in the ribosome, on engineering it into the SAM-I riboswitch, it changes to the N3 structure, resulting in a significant alteration in the trajectory of the helical arms.

The plasticity of a structural motif in RNA: Structural polymorphism of a kink turn as a function of its environment.,Daldrop P, Lilley DM RNA. 2013 Jan 16. PMID:23325110[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Daldrop P, Lilley DM. The plasticity of a structural motif in RNA: Structural polymorphism of a kink turn as a function of its environment. RNA. 2013 Jan 16. PMID:23325110 doi:http://dx.doi.org/10.1261/rna.036657.112

4b5r, resolution 2.95Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA