2n6x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2n6x" [edit=sysop:move=sysop])
Current revision (09:56, 14 June 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 2n6x is ON HOLD
+
==NMR Assignment and structure of CssA5 (middle region) of CssA thermometer from Neisseria meningitidis==
 +
<StructureSection load='2n6x' size='340' side='right'caption='[[2n6x]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2n6x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N6X FirstGlance]. <br>
 +
</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=2n6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n6x OCA], [https://pdbe.org/2n6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n6x RCSB], [https://www.ebi.ac.uk/pdbsum/2n6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n6x ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Neisseria meningitidis causes bacterial meningitis and septicemia. It evades the host complement system by upregulating expression of immune evasion factors in response to changes in temperature. RNA thermometers within mRNAs control expression of bacterial immune evasion factors, including CssA, in the 5'-untranslated region of the operon for capsule biosynthesis. We dissect the molecular mechanisms of thermoregulation and report the structure of the CssA thermometer. We show that the RNA thermometer acts as a rheostat, whose stability is optimized to respond in a small temperature range around 37 degrees C as occur within the upper airways during infection. Small increases in temperature gradually open up the structure to allow progressively increased access to the ribosome binding site. Even small changes in stability induced by mutations of imperfect base pairs, as in naturally occurring polymorphisms, shift the thermometer response outside of the desired temperature range, suggesting that its activity could be modulated by pharmacological intervention.
-
Authors: Barnwal, R., Godin, K., Varani, G.
+
Structure and mechanism of a molecular rheostat, an RNA thermometer that modulates immune evasion by Neisseria meningitidis.,Barnwal RP, Loh E, Godin KS, Yip J, Lavender H, Tang CM, Varani G Nucleic Acids Res. 2016 Jul 1. pii: gkw584. PMID:27369378<ref>PMID:27369378</ref>
-
Description: NMR Assignment and structure of CssA5 (middle region) of CssA thermometer from Neisseria meningitidis
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Varani, G]]
+
<div class="pdbe-citations 2n6x" style="background-color:#fffaf0;"></div>
-
[[Category: Godin, K]]
+
== References ==
-
[[Category: Barnwal, R]]
+
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Neisseria meningitidis]]
 +
[[Category: Barnwal R]]
 +
[[Category: Godin K]]
 +
[[Category: Varani G]]

Current revision

NMR Assignment and structure of CssA5 (middle region) of CssA thermometer from Neisseria meningitidis

PDB ID 2n6x

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools