4K1P

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

Summary for 4K1P

• Entry DOI: 10.2210/pdb4k1p/pdb
• Descriptor: NheA, 1,2-ETHANEDIOL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: helical bundle, beta tongue, clya-like fold, pore-forming toxin component, toxin
• Biological source: Bacillus cereus
• Total number of polymer chains: 8
• Total formula weight: 329095.22

Authors

Ganash, M.,Phung, D.,Artymiuk, P.J. (deposition date: 2013-04-05, release date: 2013-09-18, Last modification date: 2024-02-28)

Primary citation

Ganash, M.,Phung, D.,Sedelnikova, S.E.,Lindback, T.,Granum, P.E.,Artymiuk, P.J.
Structure of the NheA Component of the Nhe Toxin from Bacillus cereus: Implications for Function.
Plos One, 8:e74748-e74748, 2013

PubMed Abstract: The structure of NheA, a component of the Bacillus cereus Nhe tripartite toxin, has been solved at 2.05 Å 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 α-helical pore forming toxins (α-PFTs), although its head domain is significantly enlarged compared with those of ClyA or Hbl-B. The hydrophobic β-hairpin structure that is a characteristic of these toxins is replaced by an amphipathic β-hairpin connected to the main structure via a β-latch that is reminiscent of a similar structure in the β-PFT Staphylococcus aureus α-hemolysin. Taken together these results suggest that, although it is a member of an archetypal α-PFT family of toxins, NheA may be capable of forming a β rather than an α pore.

PubMed: 24040335
DOI: 10.1371/journal.pone.0074748

Experimental method

X-RAY DIFFRACTION (2.05 Å)