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1r4q

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(New page: 200px<br /><applet load="1r4q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r4q, resolution 2.50&Aring;" /> '''Shiga toxin'''<br />...)
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[[Image:1r4q.gif|left|200px]]<br /><applet load="1r4q" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1r4q, resolution 2.50&Aring;" />
 
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'''Shiga toxin'''<br />
 
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==Overview==
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==Shiga toxin==
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Several serotypes of Escherichia coli produce protein toxins closely, related to Shiga toxin (Stx) from Shigella dysenteriae serotype 1. These, Stx-producing E. coli cause outbreaks of hemorrhagic colitis and hemolytic, uremic syndrome in humans, with the latter being more likely if the E., coli produce Stx2 than if they only produce Stx1. To investigate the, differences among the Stxs, which are all AB(5) toxins, the crystal, structure of Stx2 from E. coli O157:H7 was determined at 1.8-A resolution, and compared with the known structure of Stx. Our major finding was that, in contrast to Stx, the active site of the A-subunit of Stx2 is accessible, in the holotoxin, and a molecule of formic acid and a water molecule mimic, the binding of the adenine base of the substrate. Further, the A-subunit, adopts a different orientation with respect to the B-subunits in Stx2 than, in Stx, due to interactions between the carboxyl termini of the B-subunits, and neighboring regions of the A-subunit. Of the three types of, receptor-binding sites in the B-pentamer, one has a different conformation, in Stx2 than in Stx, and the carboxyl terminus of the A-subunit binds at, another. Any of these structural differences might result in different, mechanisms of action of the two toxins and the development of hemolytic, uremic syndrome upon exposure to Stx2.
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<StructureSection load='1r4q' size='340' side='right'caption='[[1r4q]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1r4q]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_dysenteriae Shigella dysenteriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R4Q FirstGlance]. <br>
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4q OCA], [https://pdbe.org/1r4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r4q RCSB], [https://www.ebi.ac.uk/pdbsum/1r4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4q ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/STXA_SHIDY STXA_SHIDY] The A subunit is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits. After endocytosis, the A subunit is cleaved by furin in two fragments, A1 and A2: A1 is the catalytically active fragment, and A2 is essential for holotoxin assembly with the B subunits.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r4/1r4q_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r4q ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1R4Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Shigella_dysenteriae Shigella dysenteriae]. Active as [http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R4Q OCA].
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*[[Shiga toxin 3D structures|Shiga toxin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of shiga toxin type 2 (Stx2) from Escherichia coli O157:H7., Fraser ME, Fujinaga M, Cherney MM, Melton-Celsa AR, Twiddy EM, O'Brien AD, James MN, J Biol Chem. 2004 Jun 25;279(26):27511-7. Epub 2004 Apr 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15075327 15075327]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Shigella dysenteriae]]
[[Category: Shigella dysenteriae]]
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[[Category: rRNA N-glycosylase]]
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[[Category: Cherney MM]]
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[[Category: Brien, A.D.O.]]
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[[Category: Fraser ME]]
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[[Category: Cherney, M.M.]]
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[[Category: Fujinaga M]]
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[[Category: Fraser, M.E.]]
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[[Category: James MNG]]
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[[Category: Fujinaga, M.]]
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[[Category: Melton-Celsa AR]]
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[[Category: James, M.N.G.]]
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[[Category: O'Brien AD]]
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[[Category: Melton-Celsa, A.R.]]
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[[Category: Twiddy EM]]
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[[Category: Twiddy, E.M.]]
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[[Category: ab5 toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:08:22 2007''
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Current revision

Shiga toxin

PDB ID 1r4q

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