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26 April 2024 |
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Article overview
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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 | 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 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 | Services: | Forum | Review | Favorites |
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