Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2QP2

Structure of a MACPF/perforin-like protein

Summary for 2QP2
Entry DOI10.2210/pdb2qp2/pdb
DescriptorUnknown protein, CALCIUM ION (3 entities in total)
Functional Keywordstoxin, unknown function
Biological sourcePhotorhabdus luminescens subsp. laumondii
Total number of polymer chains1
Total formula weight57244.83
Authors
Primary citationRosado, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon