4px8: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4px8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4px8 OCA], [http://pdbe.org/4px8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4px8 RCSB], [http://www.ebi.ac.uk/pdbsum/4px8 PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Bacteria contain multiple type II toxins that selectively degrade mRNAs bound to the ribosome to regulate translation and growth and facilitate survival during the stringent response. Ribosome-dependent toxins recognize a variety of three-nucleotide codons within the aminoacyl (A) site, but how these endonucleases achieve substrate specificity remains poorly understood. Here, we identify the critical features for how the host inhibition of growth B (HigB) toxin recognizes each of the three A-site nucleotides for cleavage. X-ray crystal structures of HigB bound to two different codons on the ribosome illustrate how HigB uses a microbial RNase-like nucleotide recognition loop to recognize either cytosine or adenosine at the second A-site position. Strikingly, a single HigB residue and 16S rRNA residue C1054 form an adenosine-specific pocket at the third A-site nucleotide, in contrast to how tRNAs decode mRNA. Our results demonstrate that the most important determinant for mRNA cleavage by ribosome-dependent toxins is interaction with the third A-site nucleotide.

Defining the mRNA recognition signature of a bacterial toxin protein.,Schureck MA, Dunkle JA, Maehigashi T, Miles SJ, Dunham CM Proc Natl Acad Sci U S A. 2015 Nov 10;112(45):13862-7. doi:, 10.1073/pnas.1512959112. Epub 2015 Oct 27. PMID:26508639<ref>PMID:26508639</ref>

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

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 7: / Line 7: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4px8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4px8 OCA], [http://pdbe.org/4px8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4px8 RCSB], [http://www.ebi.ac.uk/pdbsum/4px8 PDBsum]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bacteria contain multiple type II toxins that selectively degrade mRNAs bound to the ribosome to regulate translation and growth and facilitate survival during the stringent response. Ribosome-dependent toxins recognize a variety of three-nucleotide codons within the aminoacyl (A) site, but how these endonucleases achieve substrate specificity remains poorly understood. Here, we identify the critical features for how the host inhibition of growth B (HigB) toxin recognizes each of the three A-site nucleotides for cleavage. X-ray crystal structures of HigB bound to two different codons on the ribosome illustrate how HigB uses a microbial RNase-like nucleotide recognition loop to recognize either cytosine or adenosine at the second A-site position. Strikingly, a single HigB residue and 16S rRNA residue C1054 form an adenosine-specific pocket at the third A-site nucleotide, in contrast to how tRNAs decode mRNA. Our results demonstrate that the most important determinant for mRNA cleavage by ribosome-dependent toxins is interaction with the third A-site nucleotide.
+Defining the mRNA recognition signature of a bacterial toxin protein.,Schureck MA, Dunkle JA, Maehigashi T, Miles SJ, Dunham CM Proc Natl Acad Sci U S A. 2015 Nov 10;112(45):13862-7. doi:, 10.1073/pnas.1512959112. Epub 2015 Oct 27. PMID:26508639<ref>PMID:26508639</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4px8" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>