TY - JOUR
T1 - A common fold mediates vertebrate defense and bacterial attack
AU - Rosado, Carlos Joaquim
AU - Buckle, Ashley Maurice
AU - Law, Ruby Hong Ping
AU - Butcher, Rebecca Elizabeth
AU - Kan, Wan-Ting
AU - Bird, Catherina Hedwig
AU - Ung, Kheng Sok
AU - Browne, Kylie A
AU - Baran, Katherine
AU - Bashtannyk-Puhalovich, Tanya Ann
AU - Faux, Noel Garry
AU - Wong, Wilson
AU - Porter, Corrine Joy
AU - Pike, Robert Neil
AU - Ellisdon, Andrew Malcolm
AU - Pearce, Mary Catherine
AU - Bottomley, Stephen Paul
AU - Emsley, Jonas
AU - Smith, Alexander Ian
AU - Rossjohn, Jamie
AU - Hartland, Elizabeth Louise
AU - Voskoboinik, Ilia
AU - Trapani, Joseph A
AU - Bird, Phillip Ian
AU - Dunstone, Michelle Anne
AU - Whisstock, James
PY - 2007
Y1 - 2007
N2 - Proteins containing Membrane Attack Complex / Perforin (MACPF) domains play important roles in vertebrate immunity, embryonic development and neural cell migration. In vertebrates, C9 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 A resolution. The MACPF domain reveals structural similarity with pore forming 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 suggest that the fold of the CDCs, a family of proteins important for bacterial pathogenesis, is likely used by vertebrates for defence against infection.
AB - Proteins containing Membrane Attack Complex / Perforin (MACPF) domains play important roles in vertebrate immunity, embryonic development and neural cell migration. In vertebrates, C9 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 A resolution. The MACPF domain reveals structural similarity with pore forming 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 suggest that the fold of the CDCs, a family of proteins important for bacterial pathogenesis, is likely used by vertebrates for defence against infection.
UR - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17717151
M3 - Article
SN - 0036-8075
VL - 317
SP - 1548
EP - 1551
JO - Science
JF - Science
IS - 5844
ER -