2QP2

Structure of a MACPF/perforin-like protein

Summary for 2QP2

• Entry DOI: 10.2210/pdb2qp2/pdb
• Descriptor: Unknown protein, CALCIUM ION (3 entities in total)
• Functional Keywords: toxin, unknown function
• Biological source: Photorhabdus luminescens subsp. laumondii
• Total number of polymer chains: 1
• Total formula weight: 57244.83

Authors

Rosado, C.J.,Buckle, A.M.,Law, R.H.P.,Butcher, R.E.,Kan, W.T.,Bird, C.H.,Ung, K.,Browne, K.A.,Baran, K.,Bashtannyk-Puhalovich, T.A.,Faux, N.G.,Wong, W.,Porter, C.J.,Pike, R.N.,Ellisdon, A.M.,Pearce, M.C.,Bottomley, S.P.,Emsley, J.,Smith, A.I.,Rossjohn, J.,Hartland, E.L.,Voskoboinik, I.,Trapani, J.A.,Bird, P.I.,Dunstone, M.A.,Whisstock, J.C. (deposition date: 2007-07-22, release date: 2007-09-04, Last modification date: 2024-03-13)

Primary citation

Rosado, C.J.,Buckle, A.M.,Law, R.H.,Butcher, R.E.,Kan, W.T.,Bird, C.H.,Ung, K.,Browne, K.A.,Baran, K.,Bashtannyk-Puhalovich, T.A.,Faux, N.G.,Wong, W.,Porter, C.J.,Pike, R.N.,Ellisdon, A.M.,Pearce, M.C.,Bottomley, S.P.,Emsley, J.,Smith, A.I.,Rossjohn, J.,Hartland, E.L.,Voskoboinik, I.,Trapani, J.A.,Bird, P.I.,Dunstone, M.A.,Whisstock, J.C.
A common fold mediates vertebrate defense and bacterial attack
Science, 317:1548-1551, 2007

PubMed 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.

PubMed: 17717151
DOI: 10.1126/science.1144706

Experimental method

X-RAY DIFFRACTION (2 Å)