3M2L

Crystal structure of the M113F mutant of alpha-hemolysin

Summary for 3M2L

• Entry DOI: 10.2210/pdb3m2l/pdb
• Descriptor: Alpha-hemolysin (2 entities in total)
• Functional Keywords: beta barrel, pore-forming toxin, cytolysis, hemolysis, secreted, toxin
• Biological source: Staphylococcus aureus
• Cellular location: Secreted: P09616
• Total number of polymer chains: 7
• Total formula weight: 234060.23

Authors

Montoya, M.,Gouaux, E. (deposition date: 2010-03-07, release date: 2010-05-12, Last modification date: 2024-02-21)

Primary citation

Banerjee, A.,Mikhailova, E.,Cheley, S.,Gu, L.Q.,Montoya, M.,Nagaoka, Y.,Gouaux, E.,Bayley, H.
Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores.
Proc.Natl.Acad.Sci.USA, 107:8165-8170, 2010

PubMed Abstract: Engineered protein pores have several potential applications in biotechnology: as sensor elements in stochastic detection and ultrarapid DNA sequencing, as nanoreactors to observe single-molecule chemistry, and in the construction of nano- and micro-devices. One important class of pores contains molecular adapters, which provide internal binding sites for small molecules. Mutants of the alpha-hemolysin (alphaHL) pore that bind the adapter beta-cyclodextrin (betaCD) approximately 10(4) times more tightly than the wild type have been obtained. We now use single-channel electrical recording, protein engineering including unnatural amino acid mutagenesis, and high-resolution x-ray crystallography to provide definitive structural information on these engineered protein nanopores in unparalleled detail.

PubMed: 20400691
DOI: 10.1073/pnas.0914229107

Experimental method

X-RAY DIFFRACTION (2.1 Å)