Journal article
A common fold mediates vertebrate defense and bacterial attack
Carlos J Rosado, Ashley M Buckle, Ruby HP Law, Rebecca E Butcher, Wan-Ting Kan, Catherina H Bird, Kheng Ung, Kylie A Browne, Katherine Baran, Tanya A Bashtannyk-Puhalovich, Noel G Faux, Wilson Wong, Corrine J Porter, Robert N Pike, Andrew M Ellisdon, Mary C Pearce, Stephen P Bottomley, Jonas Emsley, A Ian Smith, Jamie Rossjohn Show all
SCIENCE | AMER ASSOC ADVANCEMENT SCIENCE | Published : 2007
Abstract
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 mechani..
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