A Common Fold Mediates Vertebrate Defense and Bacterial Attack Export

@article{citeulike:1668123, 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. 10.1126/science.1144706}, author = {Rosado, Carlos J. and Buckle, Ashley M. and Law, Ruby H. and Butcher, Rebecca E. and Kan, Wan-Ting and Bird, Catherina H. and Ung, Kheng and Browne, Kylie A. and Baran, Katherine and Bashtannyk-Puhalovich, Tanya A. and Faux, Noel G. and Wong, Wilson and Porter, Corrine J. and Pike, Robert N. and Ellisdon, Andrew M. and Pearce, Mary C. and Bottomley, Stephen P. and Emsley, Jonas and Smith, Ian A. and Rossjohn, Jamie and Hartland, Elizabeth L. and Voskoboinik, Ilia and Trapani, Joseph A. and Bird, Phillip I. and Dunstone, Michelle A. and Whisstock, James C.}, citeulike-article-id = {1668123}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1144706}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/317/5844/1548}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/17717151}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=17717151}, day = {14}, doi = {10.1126/science.1144706}, journal = {Science}, keywords = {greenbeard, immunity}, month = {September}, number = {5844}, pages = {1548--1551}, posted-at = {2007-09-18 07:15:01}, priority = {2}, title = {A Common Fold Mediates Vertebrate Defense and Bacterial Attack}, url = {http://dx.doi.org/10.1126/science.1144706}, volume = {317}, year = {2007} }

TY - JOUR ID - citeulike:1668123 L3 - citeulike-article-id:1668123 N2 - 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. 10.1126/science.1144706 IS - 5844 JF - Science EP - 1551 TI - A Common Fold Mediates Vertebrate Defense and Bacterial Attack VL - 317 SP - 1548 KW - greenbeard KW - immunity AU - Rosado, Carlos AU - Buckle, Ashley AU - Law, Ruby AU - Butcher, Rebecca AU - Kan, Wan-Ting AU - Bird, Catherina AU - Ung, Kheng AU - Browne, Kylie AU - Baran, Katherine AU - Bashtannyk-Puhalovich, Tanya AU - Faux, Noel AU - Wong, Wilson AU - Porter, Corrine AU - Pike, Robert AU - Ellisdon, Andrew AU - Pearce, Mary AU - Bottomley, Stephen AU - Emsley, Jonas AU - Smith, Ian AU - Rossjohn, Jamie AU - Hartland, Elizabeth AU - Voskoboinik, Ilia AU - Trapani, Joseph AU - Bird, Phillip AU - Dunstone, Michelle AU - Whisstock, James PY - 2007/09/14/ UR - http://dx.doi.org/10.1126/science.1144706 ER -