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| | <StructureSection load='6zi0' size='340' side='right'caption='[[6zi0]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='6zi0' size='340' side='right'caption='[[6zi0]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6zi0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Haei8 Haei8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZI0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZI0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zi0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_86-028NP Haemophilus influenzae 86-028NP]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZI0 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">vapD, NTHI0577 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=281310 HAEI8])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zi0 OCA], [http://pdbe.org/6zi0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zi0 RCSB], [http://www.ebi.ac.uk/pdbsum/6zi0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zi0 ProSAT]</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=6zi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zi0 OCA], [https://pdbe.org/6zi0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zi0 RCSB], [https://www.ebi.ac.uk/pdbsum/6zi0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zi0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q4QN95_HAEI8 Q4QN95_HAEI8]] Cleaves ssRNA, mostly between U:A.[PIRNR:PIRNR002882] | + | [https://www.uniprot.org/uniprot/Q4QN95_HAEI8 Q4QN95_HAEI8] Cleaves ssRNA, mostly between U:A.[PIRNR:PIRNR002882] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Haei8]] | + | [[Category: Haemophilus influenzae 86-028NP]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bertelsen, M B]] | + | [[Category: Bertelsen MB]] |
| - | [[Category: Bisiak, F]] | + | [[Category: Bisiak F]] |
| - | [[Category: Brodersen, D E]] | + | [[Category: Brodersen DE]] |
| - | [[Category: Cunha, M V]] | + | [[Category: Cunha MV]] |
| - | [[Category: Daines, D A]] | + | [[Category: Daines DA]] |
| - | [[Category: Molinaro, A L]] | + | [[Category: Molinaro AL]] |
| - | [[Category: Nielsen, M H]] | + | [[Category: Nielsen MH]] |
| - | [[Category: Senissar, M]] | + | [[Category: Senissar M]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nucleic-acid binding protein]]
| + | |
| - | [[Category: Rnase]]
| + | |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Toxin-antitoxin]]
| + | |
| - | [[Category: Vapxd]]
| + | |
| Structural highlights
Function
Q4QN95_HAEI8 Cleaves ssRNA, mostly between U:A.[PIRNR:PIRNR002882]
Publication Abstract from PubMed
Bacterial type II toxin-antitoxin (TA) modules encode a toxic protein that downregulates metabolism and a specific antitoxin that binds and inhibits the toxin during normal growth. In non-typeable Haemophilus influenzae, a common cause of infections in humans, the vapXD locus was found to constitute a functional TA module and contribute to pathogenicity; however, the mode of action of VapD and the mechanism of inhibition by the VapX antitoxin remain unknown. Here, we report the structure of the intact H. influenzae VapXD complex, revealing an unusual 2:1 TA molecular stoichiometry where a Cas2-like homodimer of VapD binds a single VapX antitoxin. VapX consists of an oligonucleotide/oligosaccharide-binding domain that docks into an asymmetrical cavity on the toxin dimer. Structures of isolated VapD further reveal how a symmetrical toxin homodimer adapts to interacting with an asymmetrical antitoxin and suggest how a primordial TA system evolved to become part of CRISPR-Cas immunity systems.
Structural Basis for Toxin Inhibition in the VapXD Toxin-Antitoxin System.,Bertelsen MB, Senissar M, Nielsen MH, Bisiak F, Cunha MV, Molinaro AL, Daines DA, Brodersen DE Structure. 2020 Oct 16. pii: S0969-2126(20)30373-7. doi:, 10.1016/j.str.2020.10.002. PMID:33096014[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bertelsen MB, Senissar M, Nielsen MH, Bisiak F, Cunha MV, Molinaro AL, Daines DA, Brodersen DE. Structural Basis for Toxin Inhibition in the VapXD Toxin-Antitoxin System. Structure. 2020 Oct 16. pii: S0969-2126(20)30373-7. doi:, 10.1016/j.str.2020.10.002. PMID:33096014 doi:http://dx.doi.org/10.1016/j.str.2020.10.002
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