4k1p

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==Structure of the NheA component of the Nhe toxin from Bacillus cereus==
==Structure of the NheA component of the Nhe toxin from Bacillus cereus==
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<StructureSection load='4k1p' size='340' side='right' caption='[[4k1p]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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<StructureSection load='4k1p' size='340' side='right'caption='[[4k1p]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4k1p]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K1P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4k1p]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K1P FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 2.05&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nheA, nheABC (operon) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 ATCC 14579])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=4k1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k1p OCA], [http://pdbe.org/4k1p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k1p RCSB], [http://www.ebi.ac.uk/pdbsum/4k1p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k1p ProSAT]</span></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=4k1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k1p OCA], [https://pdbe.org/4k1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k1p RCSB], [https://www.ebi.ac.uk/pdbsum/4k1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k1p ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q3Y6N6_BACCE Q3Y6N6_BACCE]
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The structure of NheA, a component of the Bacillus cereus Nhe tripartite toxin, has been solved at 2.05 A resolution using selenomethionine multiple-wavelength anomalous dispersion (MAD). The structure shows it to have a fold that is similar to the Bacillus cereus Hbl-B and E. coli ClyA toxins, and it is therefore a member of the ClyA superfamily of alpha-helical pore forming toxins (alpha-PFTs), although its head domain is significantly enlarged compared with those of ClyA or Hbl-B. The hydrophobic beta-hairpin structure that is a characteristic of these toxins is replaced by an amphipathic beta-hairpin connected to the main structure via a beta-latch that is reminiscent of a similar structure in the beta-PFT Staphylococcus aureus alpha-hemolysin. Taken together these results suggest that, although it is a member of an archetypal alpha-PFT family of toxins, NheA may be capable of forming a beta rather than an alpha pore.
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Structure of the NheA Component of the Nhe Toxin from Bacillus cereus: Implications for Function.,Ganash M, Phung D, Sedelnikova SE, Lindback T, Granum PE, Artymiuk PJ PLoS One. 2013 Sep 10;8(9):e74748. doi: 10.1371/journal.pone.0074748. PMID:24040335<ref>PMID:24040335</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4k1p" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 14579]]
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[[Category: Bacillus cereus]]
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[[Category: Artymiuk, P J]]
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[[Category: Large Structures]]
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[[Category: Ganash, M]]
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[[Category: Artymiuk PJ]]
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[[Category: Phung, D]]
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[[Category: Ganash M]]
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[[Category: Beta tongue]]
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[[Category: Phung D]]
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[[Category: Clya-like fold]]
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[[Category: Helical bundle]]
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[[Category: Pore-forming toxin component]]
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[[Category: Toxin]]
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Current revision

Structure of the NheA component of the Nhe toxin from Bacillus cereus

PDB ID 4k1p

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