Crystal structure of octameric pore form of gamma-hemolysin from Staphylococcus aureus
The structure was published by Yamashita, K., Kawai, Y., Tanaka, Y., et al., Kamio, Y., Yao, M., and Tanaka, I., in 2011 in a paper entitled "Crystal structure of the octameric pore of staphylococcal gamma-hemolysin reveals the beta-barrel pore formation mechanism by two components" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.495 Å and deposited in 2011.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely Gamma-hemolysin component B and Gamma-hemolysin component A.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms heterooctamers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 2 unique UniProt proteins: