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| | <StructureSection load='4px8' size='340' side='right'caption='[[4px8]], [[Resolution|resolution]] 1.25Å' scene=''> | | <StructureSection load='4px8' size='340' side='right'caption='[[4px8]], [[Resolution|resolution]] 1.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4px8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PX8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4px8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PX8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mct|4mct]], [[4mcx|4mcx]], [[4pxr|4pxr]], [[4w4g|4w4g]], [[4ypb|4ypb]], [[4yzv|4yzv]]</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=4px8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4px8 OCA], [https://pdbe.org/4px8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4px8 RCSB], [https://www.ebi.ac.uk/pdbsum/4px8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4px8 ProSAT]</span></td></tr> |
| - | <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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4px8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HIGB_PROVU HIGB_PROVU] Toxic component of a type II toxin-antitoxin (TA) module (PubMed:19423702, PubMed:24257752, PubMed:8645296). A ribosome-associated translation-dependent mRNA interferase. Inhibits translation by sequence-specific cleavage of mRNA. Prefers either in-frame or out-of-frame 5'-AAA-3' codons (lysine). Cleaves also the first three AAAs of stretches of four or more A sequences. 20% of codons containing AA are cleaved and occassionally cuts even at a single A (PubMed:19423702).<ref>PMID:19423702</ref> <ref>PMID:24257752</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dunham, C M]] | + | [[Category: Proteus vulgaris]] |
| - | [[Category: Dunkle, J A]] | + | [[Category: Dunham CM]] |
| - | [[Category: Maehigashi, T]] | + | [[Category: Dunkle JA]] |
| - | [[Category: Schureck, M A]] | + | [[Category: Maehigashi T]] |
| - | [[Category: And ribosome]] | + | [[Category: Schureck MA]] |
| - | [[Category: Bacterial toxin]]
| + | |
| - | [[Category: Biofilm]]
| + | |
| - | [[Category: Cell metabolism]]
| + | |
| - | [[Category: Energy metabolism]]
| + | |
| - | [[Category: Host inhibition of growth some]]
| + | |
| - | [[Category: Microbial pathogenesis]]
| + | |
| - | [[Category: Microbial rnase fold]]
| + | |
| - | [[Category: Mrna]]
| + | |
| - | [[Category: Ribosome-dependent mrna interferase]]
| + | |
| - | [[Category: Stress response]]
| + | |
| - | [[Category: Stringent response]]
| + | |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Translation control]]
| + | |
| Structural highlights
Function
HIGB_PROVU Toxic component of a type II toxin-antitoxin (TA) module (PubMed:19423702, PubMed:24257752, PubMed:8645296). A ribosome-associated translation-dependent mRNA interferase. Inhibits translation by sequence-specific cleavage of mRNA. Prefers either in-frame or out-of-frame 5'-AAA-3' codons (lysine). Cleaves also the first three AAAs of stretches of four or more A sequences. 20% of codons containing AA are cleaved and occassionally cuts even at a single A (PubMed:19423702).[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hurley JM, Woychik NA. Bacterial toxin HigB associates with ribosomes and mediates translation-dependent mRNA cleavage at A-rich sites. J Biol Chem. 2009 Jul 10;284(28):18605-13. doi: 10.1074/jbc.M109.008763. Epub, 2009 May 7. PMID:19423702 doi:http://dx.doi.org/10.1074/jbc.M109.008763
- ↑ Schureck MA, Maehigashi T, Miles SJ, Marquez J, Ei Cho S, Erdman R, Dunham CM. Structure of the P. vulgaris HigB-(HigA)2-HigB toxin-antitoxin complex. J Biol Chem. 2013 Nov 20. PMID:24257752 doi:http://dx.doi.org/10.1074/jbc.M113.512095
- ↑ Schureck MA, Dunkle JA, Maehigashi T, Miles SJ, Dunham CM. Defining the mRNA recognition signature of a bacterial toxin protein. 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 doi:http://dx.doi.org/10.1073/pnas.1512959112
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