4k1p | pdb_00004k1p

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

spinqualitylabelsall models 4k1p, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4k1p is a 8 chain structure with sequence from Bacillus cereus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3Y6N6_BACCE 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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