Monash University ARROW Repository | 2QP2 - Structure of a MACPF/Perforin-like protein

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Buckle Ashley M, Law Ruby H. P., Whisstock James C., Dunstone Michelle A.. 2QP2 - Structure of a MACPF/Perforin-like protein.

Please use this identifier to cite or link to this item: http://arrow.monash.edu.au/hdl/1959.1/42179

Title: 2QP2 - Structure of a MACPF/Perforin-like protein
Creator: Buckle Ashley M
Creator: Law Ruby H. P.
Creator: Whisstock James C.
Creator: Dunstone Michelle A.
Description: Protein crystallography raw diffraction images and unmerged reflection intensities Collection size: 36.1 GB Number of datasets: 5 Citation: Rosado et. al. (2007) A common fold mediates vertebrate defense and bacterial attack. Science. In Press. Proteins containing membrane attack complex/perforin (MACPF) domains play important roles in vertebrate immunity, embryonic development, and neural-cell migration. In vertebrates, the ninth component of complement and perforin form oligomeric pores that lyse bacteria and kill virus-infected cells, respectively. However, the mechanism of MACPF function is unknown. We determined the crystal structure of a bacterial MACPF protein, Plu-MACPF from Photorhabdus luminescens, to 2.0 angstrom resolution. The MACPF domain reveals structural similarity with poreforming cholesterol-dependent cytolysins (CDCs) from Gram-positive bacteria. This suggests that lytic MACPF proteins may use a CDC-like mechanism to form pores and disrupt cell membranes. Sequence similarity between bacterial and vertebrate MACPF domains suggests that the fold of the CDCs, a family of proteins important for bacterial pathogenesis, is probably used by vertebrates for defense against infection.

File	Description	Size	Format
MARCDESC	MARCXML Record	2 KB	XML Document	View Details	Download
oai_ds	TARDIS XML: oai_ds	9 KB	XML Document	View Details	Download

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