2N67
C-terminal domain of Hemolysin II-P87M-BMRB
Summary for 2N67
| Entry DOI | 10.2210/pdb2n67/pdb |
| NMR Information | BMRB: 19463 |
| Descriptor | Hemolysin II (1 entity in total) |
| Functional Keywords | hemolysin, novel fold, pore-forming toxin, conformational heterogeneity, toxin |
| Biological source | Bacillus cereus |
| Total number of polymer chains | 1 |
| Total formula weight | 10461.71 |
| Authors | Kaplan, A.R.,Maciejewski, M.W.,Olson, R.,Alexandrescu, A.T. (deposition date: 2015-08-13, release date: 2016-08-17, Last modification date: 2024-05-15) |
| Primary citation | Kaplan, A.R.,Kaus, K.,De, S.,Olson, R.,Alexandrescu, A.T. NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold. Sci Rep, 7:3277-3277, 2017 Cited by PubMed Abstract: In addition to multiple virulence factors, Bacillus cereus a pathogen that causes food poisoning and life-threatening wound infections, secretes the pore-forming toxin hemolysin II (HlyII). The HlyII toxin has a unique 94 amino acid C-terminal domain (HlyIIC). HlyIIC exhibits splitting of NMR resonances due to cis/trans isomerization of a single proline near the C-terminus. To overcome heterogeneity, we solved the structure of P405M-HlyIIC, a mutant that exclusively stabilizes the trans state. The NMR structure of HlyIIC reveals a novel fold, consisting of two subdomains αA-β1-β2 and β3-β4-αB-β5, that come together in a barrel-like structure. The barrel core is fastened by three layers of hydrophobic residues. The barrel end opposite the HlyIIC-core has a positively charged surface, that by binding negatively charged moieties on cellular membranes, may play a role in target-cell surface recognition or stabilization of the heptameric pore complex. In the WT domain, dynamic flexibility occurs at the N-terminus and the first α-helix that connects the HlyIIC domain to the HlyII-core structure. In the destabilizing P405M mutant, increased flexibility is evident throughout the first subdomain, suggesting that the HlyIIC structure may have arisen through gene fusion. PubMed: 28607368DOI: 10.1038/s41598-017-02917-4 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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