2h28

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of YeeU from E. coli. Northeast Structural Genomics target ER304

Structural highlights

2h28 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

CBEA_ECOLI Antitoxin component of a type IV toxin-antitoxin (TA) module. Labile antitoxin that counteracts the effect of its cognate toxin CbtA (YeeV). It does not bind to the toxin but instead binds to MreB and FtsZ (the toxin targets), enhancing their polymerization by forming higher-order bundles; it is probably retained in the MreB and FtsZ filament bundles. The mechanism has been proposed to require intergenic DNA, in cis, between the cbeA (yeeU) and cbta (yeeV) genes (PubMed:14594833). The intergenic region was not found to be necessary in another study (PubMed:22515815). Also counteracts the morphological defects caused by overexpression of SulA and DicB on cell shape.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bacterial toxin-antitoxin (TA) systems serve a variety of physiological functions including regulation of cell growth and maintenance of foreign genetic elements. Sequence analyses suggest that TA families are linked by complex evolutionary relationships reflecting likely swapping of functional domains between different TA families. Our crystal structures of Phd-Doc from bacteriophage P1, the HigA antitoxin from Escherichia coli CFT073, and YeeU of the YeeUWV systems from E. coli K12 and Shigella flexneri confirm this inference and reveal additional, unanticipated structural relationships. The growth-regulating Doc toxin exhibits structural similarity to secreted virulence factors that are toxic for eukaryotic target cells. The Phd antitoxin possesses the same fold as both the YefM and NE2111 antitoxins that inhibit structurally unrelated toxins. YeeU, which has an antitoxin-like activity that represses toxin expression, is structurally similar to the ribosome-interacting toxins YoeB and RelE. These observations suggest extensive functional exchanges have occurred between TA systems during bacterial evolution.

Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems.,Arbing MA, Handelman SK, Kuzin AP, Verdon G, Wang C, Su M, Rothenbacher FP, Abashidze M, Liu M, Hurley JM, Xiao R, Acton T, Inouye M, Montelione GT, Woychik NA, Hunt JF Structure. 2010 Aug 11;18(8):996-1010. PMID:20696400^[3]

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

References

↑ Brown JM, Shaw KJ. A novel family of Escherichia coli toxin-antitoxin gene pairs. J Bacteriol. 2003 Nov;185(22):6600-8. PMID:14594833
↑ Masuda H, Tan Q, Awano N, Wu KP, Inouye M. YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli. Mol Microbiol. 2012 Jun;84(5):979-89. doi: 10.1111/j.1365-2958.2012.08068.x. Epub, 2012 May 17. PMID:22515815 doi:http://dx.doi.org/10.1111/j.1365-2958.2012.08068.x
↑ Arbing MA, Handelman SK, Kuzin AP, Verdon G, Wang C, Su M, Rothenbacher FP, Abashidze M, Liu M, Hurley JM, Xiao R, Acton T, Inouye M, Montelione GT, Woychik NA, Hunt JF. Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems. Structure. 2010 Aug 11;18(8):996-1010. PMID:20696400 doi:10.1016/j.str.2010.04.018

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h28"

@@ Line 3: / Line 3: @@
 <StructureSection load='2h28' size='340' side='right'caption='[[2h28]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2h28]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H28 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2h28]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H28 FirstGlance]. <br>
-</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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.1&#8491;</td></tr>
-<tr id='NonStdRes'><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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yeeU ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2h28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h28 OCA], [https://pdbe.org/2h28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h28 RCSB], [https://www.ebi.ac.uk/pdbsum/2h28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h28 ProSAT], [https://www.topsan.org/Proteins/NESGC/2h28 TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CBEA_ECOLI CBEA_ECOLI]] Antitoxin component of a type IV toxin-antitoxin (TA) module. Labile antitoxin that counteracts the effect of its cognate toxin CbtA (YeeV). It does not bind to the toxin but instead binds to MreB and FtsZ (the toxin targets), enhancing their polymerization by forming higher-order bundles; it is probably retained in the MreB and FtsZ filament bundles. The mechanism has been proposed to require intergenic DNA, in cis, between the cbeA (yeeU) and cbta (yeeV) genes (PubMed:14594833). The intergenic region was not found to be necessary in another study (PubMed:22515815). Also counteracts the morphological defects caused by overexpression of SulA and DicB on cell shape.<ref>PMID:14594833</ref> <ref>PMID:22515815</ref>
+[https://www.uniprot.org/uniprot/CBEA_ECOLI CBEA_ECOLI] Antitoxin component of a type IV toxin-antitoxin (TA) module. Labile antitoxin that counteracts the effect of its cognate toxin CbtA (YeeV). It does not bind to the toxin but instead binds to MreB and FtsZ (the toxin targets), enhancing their polymerization by forming higher-order bundles; it is probably retained in the MreB and FtsZ filament bundles. The mechanism has been proposed to require intergenic DNA, in cis, between the cbeA (yeeU) and cbta (yeeV) genes (PubMed:14594833). The intergenic region was not found to be necessary in another study (PubMed:22515815). Also counteracts the morphological defects caused by overexpression of SulA and DicB on cell shape.<ref>PMID:14594833</ref> <ref>PMID:22515815</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h28_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Acton, T B]]
+[[Category: Acton TB]]
-[[Category: Arbing, M]]
+[[Category: Arbing M]]
-[[Category: Benach, J]]
+[[Category: Benach J]]
-[[Category: Chen, C X]]
+[[Category: Chen CX]]
-[[Category: Cunningham, K]]
+[[Category: Cunningham K]]
-[[Category: Hunt, J F]]
+[[Category: Hunt JF]]
-[[Category: Jiang, M]]
+[[Category: Jiang M]]
-[[Category: Karpowich, N K]]
+[[Category: Karpowich NK]]
-[[Category: Ma, L C]]
+[[Category: Ma L-C]]
-[[Category: Montelione, G T]]
+[[Category: Montelione GT]]
-[[Category: Structural genomic]]
+[[Category: Su M]]
-[[Category: Su, M]]
+[[Category: Tong L]]
-[[Category: Tong, L]]
+[[Category: Xiao R]]
-[[Category: Xiao, R]]
-[[Category: E. coli]]
-[[Category: Er304]]
-[[Category: Nesg]]
-[[Category: PSI, Protein structure initiative]]
-[[Category: Unknown function]]

2h28

From Proteopedia

Current revision

Crystal structure of YeeU from E. coli. Northeast Structural Genomics target ER304

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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