2qp2

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Revision as of 10:41, 23 January 2008

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spinqualitylabelsall models 2qp2, resolution 2.000Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of a MACPF/perforin-like protein

Overview

Proteins containing Membrane Attack Complex / Perforin (MACPF) domains, play important roles in vertebrate immunity, embryonic development and, neural cell migration. In vertebrates, C9 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 A resolution. The MACPF domain reveals, structural similarity with pore forming 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 suggest that the fold of the CDCs, a family of proteins important, for bacterial pathogenesis, is likely used by vertebrates for defence, against infection.

About this Structure

2QP2 is a Single protein structure of sequence from Photorhabdus luminescens subsp. laumondii with as ligand. Full crystallographic information is available from OCA.

Reference

A Common Fold Mediates Vertebrate Defense and Bacterial Attack., Rosado CJ, Buckle AM, Law RH, Butcher RE, Kan WT, Bird CH, Ung K, Browne KA, Baran K, Bashtannyk-Puhalovich TA, Faux NG, Wong W, Porter CJ, Pike RN, Ellisdon AM, Pearce MC, Bottomley SP, Emsley J, Smith AI, Rossjohn J, Hartland EL, Voskoboinik I, Trapani JA, Bird PI, Dunstone MA, Whisstock JC, Science. 2007 Aug 23;. PMID:17717151

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