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26 April 2024
 
  » pubmed » pmid17717151

 Article overview



A common fold mediates vertebrate defense and bacterial attack
Carlos J Rosado ; Ashley M Buckle ; Ruby H P 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 ; Elizabeth L Hartl ; Ilia Voskoboinik ; Joseph A Trapani ; Phillip I Bird ; Michelle A Dunstone ; James C Whisstock ;
Date 14 Sep 2007
Journal Science, 317 (5844), 1548-51
AbstractProteins 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.
Source PubMed, pmid17717151 doi: 10.1126/science.1144706
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