Data

A common fold mediates vertebrate defense and bacterial attack (2QP2)

Monash University
Ashley Buckle (Aggregated by) James Whisstock (Aggregated by) Michelle Dunstone (Aggregated by)
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ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2FANDS&rft_id=info:doi10.4225/03/57428b277afc1&rft.title=A common fold mediates vertebrate defense and bacterial attack (2QP2)&rft.identifier=http://doi.org/10.4225/03/57428b277afc1&rft.publisher=Monash University&rft.description=Protein crystallography raw diffraction images and unmerged reflection intensities Collection size: 36.1 GB Number of datasets: 5 Citation: Rosado et. al. (2007) A common fold mediates vertebrate defense and bacterial attack. Science. In Press. 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.&rft.creator=Ashley Buckle&rft.creator=Ashley Buckle&rft.creator=James Whisstock&rft.creator=James Whisstock&rft.creator=Michelle Dunstone&rft.creator=Michelle Dunstone&rft.creator=Ruby Law&rft.creator=Ruby Law&rft.date=2016&rft_rights=&rft_subject=protein crystallography&rft_subject=perforin&rft_subject=imaginglocus&rft.type=dataset&rft.language=English Access the data
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Protein crystallography raw diffraction images and unmerged reflection intensities Collection size: 36.1 GB Number of datasets: 5 Citation: Rosado et. al. (2007) A common fold mediates vertebrate defense and bacterial attack. Science. In Press. 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.

Issued: 2016-12-11

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imaginglocus | perforin | protein crystallography |

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Identifiers
ACN 633 798 857