3zvk

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of VapBC2 from Rickettsia felis bound to a DNA fragment from their promoter

Structural highlights

3zvk is a 10 chain structure with sequence from Rickettsia felis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VAPC2_RICFE Toxic component of a type II toxin-antitoxin (TA) system. Has ssRNase activity. Upon expression in E.coli or S.cerevisiae inhibits growth in liquid culture; in S.cerevisiae its expression leads to apoptosis-like characteristics. Rapidly induces apoptosis (within 2 hours) upon microinjection into mouse fibroblasts (L929 line); pretreatment of cells with dexamethasone protects them. Probably contributes to host cell death if bacterial cell lysis occurs during host infection. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB2, its RNase activity is partially inhibited in vitro by VapB2 (PubMed:22046301).[HAMAP-Rule:MF_00265]^[1]

Publication Abstract from PubMed

Besides their commonly attributed role in the maintenance of low-copy number plasmids, toxin/antitoxin (TA) loci, also called 'addiction modules', have been found in chromosomes and associated to a number of biological functions such as: reduction of protein synthesis, gene regulation and retardation of cell growth under nutritional stress. The recent discovery of TA loci in obligatory intracellular species of the Rickettsia genus has prompted new research to establish whether they work as stress response elements or as addiction systems that might be toxic for the host cell. VapBC2 is a TA locus from R. felis, a pathogen responsible for flea-borne spotted fever in humans. The VapC2 toxin is a PIN-domain protein, whereas the antitoxin, VapB2, belongs to the family of swapped-hairpin beta-barrel DNA-binding proteins. We have used a combination of biophysical and structural methods to characterize this new toxin/antitoxin pair. Our results show how VapB2 can block the VapC2 toxin. They provide a first structural description of the interaction between a swapped-hairpin beta-barrel protein and DNA. Finally, these results suggest how the VapC2/VapB2 molar ratio can control the self-regulation of the TA locus transcription.

Crystal structure of the DNA-bound VapBC2 antitoxin/toxin pair from Rickettsia felis.,Mate MJ, Vincentelli R, Foos N, Raoult D, Cambillau C, Ortiz-Lombardia M Nucleic Acids Res. 2012 Apr 1;40(7):3245-58. Epub 2011 Dec 2. PMID:22140099^[2]

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

References

↑ Audoly G, Vincentelli R, Edouard S, Georgiades K, Mediannikov O, Gimenez G, Socolovschi C, Mège JL, Cambillau C, Raoult D. Effect of rickettsial toxin VapC on its eukaryotic host. PLoS One. 2011;6(10):e26528. PMID:22046301 doi:10.1371/journal.pone.0026528
↑ Mate MJ, Vincentelli R, Foos N, Raoult D, Cambillau C, Ortiz-Lombardia M. Crystal structure of the DNA-bound VapBC2 antitoxin/toxin pair from Rickettsia felis. Nucleic Acids Res. 2012 Apr 1;40(7):3245-58. Epub 2011 Dec 2. PMID:22140099 doi:10.1093/nar/gkr1167

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3zvk"

Categories: Large Structures | Rickettsia felis | Cambillau C | Mate MJ | Ortiz-Lombardia M

@@ Line 3: / Line 3: @@
 <StructureSection load='3zvk' size='340' side='right'caption='[[3zvk]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3zvk]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/"rickettsia_felis"_higgins_et_al._1996 "rickettsia felis" higgins et al. 1996]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZVK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3zvk]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Rickettsia_felis Rickettsia felis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZVK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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=3zvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zvk OCA], [https://pdbe.org/3zvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zvk RCSB], [https://www.ebi.ac.uk/pdbsum/3zvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zvk ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/Q4UNB2_RICFE Q4UNB2_RICFE]] Toxic component of a toxin-antitoxin (TA) module. An RNase (By similarity).[HAMAP-Rule:MF_00265]
+[https://www.uniprot.org/uniprot/VAPC2_RICFE VAPC2_RICFE] Toxic component of a type II toxin-antitoxin (TA) system. Has ssRNase activity. Upon expression in E.coli or S.cerevisiae inhibits growth in liquid culture; in S.cerevisiae its expression leads to apoptosis-like characteristics. Rapidly induces apoptosis (within 2 hours) upon microinjection into mouse fibroblasts (L929 line); pretreatment of cells with dexamethasone protects them. Probably contributes to host cell death if bacterial cell lysis occurs during host infection. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB2, its RNase activity is partially inhibited in vitro by VapB2 (PubMed:22046301).[HAMAP-Rule:MF_00265]<ref>PMID:22046301</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Rickettsia felis higgins et al. 1996]]
 [[Category: Large Structures]]
-[[Category: Cambillau, C]]
+[[Category: Rickettsia felis]]
-[[Category: Mate, M J]]
+[[Category: Cambillau C]]
-[[Category: Ortiz-Lombardia, M]]
+[[Category: Mate MJ]]
-[[Category: Antitoxin-toxin-dna complex]]
+[[Category: Ortiz-Lombardia M]]
-[[Category: Protein-dna complex]]

3zvk

From Proteopedia

Current revision

Crystal structure of VapBC2 from Rickettsia felis bound to a DNA fragment from their promoter

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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