4q2u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:18, 6 November 2024) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of the E. coli DinJ-YafQ toxin-antitoxin complex==
==Crystal structure of the E. coli DinJ-YafQ toxin-antitoxin complex==
-
<StructureSection load='4q2u' size='340' side='right' caption='[[4q2u]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+
<StructureSection load='4q2u' size='340' side='right'caption='[[4q2u]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4q2u]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q2U FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4q2u]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q2U FirstGlance]. <br>
-
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><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]] 1.8&#8491;</td></tr>
-
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q2u RCSB], [http://www.ebi.ac.uk/pdbsum/4q2u PDBsum]</span></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=4q2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2u OCA], [https://pdbe.org/4q2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q2u RCSB], [https://www.ebi.ac.uk/pdbsum/4q2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q2u ProSAT]</span></td></tr>
-
<table>
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/DINJ_ECOLI DINJ_ECOLI] Antitoxin component of a toxin-antitoxin (TA) module. A labile antitoxin that counteracts the effect of the YafQ toxin. YafQ and DinJ together bind their own promoter, and by analogy to other TA modules probably repress its expression.<ref>PMID:17263853</ref> <ref>PMID:19210620</ref> <ref>PMID:19707553</ref> Cell death governed by the MazE-MazF and DinJ-YafQ TA modules seems to play a role in biofilm formation.<ref>PMID:17263853</ref> <ref>PMID:19210620</ref> <ref>PMID:19707553</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Bacteria encounter environmental stresses that regulate a gene expression program required for adaptation and survival. Here, we report the 1.8 Angstrom crystal structure of the E. coli toxin-antitoxin complex YafQ-(DinJ)2-YafQ, a key component of the stress response. The antitoxin DinJ dimer adopts a ribbon-helix-helix motif required for transcriptional autorepression while toxin YafQ contains a microbial RNase fold whose proposed active site is concealed by DinJ binding. Contrary to previous reports, our studies indicate that equivalent levels of transcriptional repression occur by direct interaction of either YafQ-(DinJ)2-YafQ or a DinJ dimer at a single inverted repeat of its recognition sequence which overlaps with the -10 promoter region. Surprisingly multiple YafQ-(DinJ)2-YafQ complexes binding to the operator region do not appear to amplify the extent of repression. Our results suggest an alternative model for transcriptional autorepression that may be novel to DinJ-YafQ.
 +
 
 +
Mechanisms of Toxin Inhibition and Transcriptional Repression by E. coli DinJ-YafQ.,Ruangprasert A, Maehigashi T, Miles SJ, Giridharan N, Liu JX, Dunham CM J Biol Chem. 2014 Jun 4. pii: jbc.M114.573006. PMID:24898247<ref>PMID:24898247</ref>
 +
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 4q2u" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Dunham, C M.]]
+
[[Category: Escherichia coli K-12]]
-
[[Category: Maehigashi, T.]]
+
[[Category: Large Structures]]
-
[[Category: Ruangprasert, A.]]
+
[[Category: Dunham CM]]
-
[[Category: Bacterial toxin-antitoxin complex]]
+
[[Category: Maehigashi T]]
-
[[Category: Dna binding]]
+
[[Category: Ruangprasert A]]
-
[[Category: Rhh motif]]
+
-
[[Category: Ribonuclease]]
+
-
[[Category: Ribosome binding]]
+
-
[[Category: Toxin-toxin repressor complex]]
+
-
[[Category: Translation control]]
+

Current revision

Crystal structure of the E. coli DinJ-YafQ toxin-antitoxin complex

PDB ID 4q2u

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4q2u"
Personal tools