4k1p
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Structure of the NheA component of the Nhe toxin from Bacillus cereus== | |
| - | + | <StructureSection load='4k1p' size='340' side='right' caption='[[4k1p]], [[Resolution|resolution]] 2.05Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4k1p]] is a 8 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K1P FirstGlance]. <br> | ||
| + | </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> | ||
| + | <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 Bacillus cereus])</td></tr> | ||
| + | <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://www.rcsb.org/pdb/explore.do?structureId=4k1p RCSB], [http://www.ebi.ac.uk/pdbsum/4k1p PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
| - | [[Category: Artymiuk, P J | + | [[Category: Artymiuk, P J]] |
| - | [[Category: Ganash, M | + | [[Category: Ganash, M]] |
| - | [[Category: Phung, D | + | [[Category: Phung, D]] |
[[Category: Beta tongue]] | [[Category: Beta tongue]] | ||
[[Category: Clya-like fold]] | [[Category: Clya-like fold]] | ||
Revision as of 14:49, 21 December 2014
Structure of the NheA component of the Nhe toxin from Bacillus cereus
| |||||||||||
