2qp2
From Proteopedia
(New page: 200px<br /><applet load="2qp2" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qp2, resolution 2.000Å" /> '''Structure of a MACP...) |
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==Overview== | ==Overview== | ||
| - | Proteins containing | + | 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. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | A | + | 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 Sep 14;317(5844):1548-51. Epub 2007 Aug 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17717151 17717151] |
[[Category: Photorhabdus luminescens subsp. laumondii]] | [[Category: Photorhabdus luminescens subsp. laumondii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Baran, K.]] | [[Category: Baran, K.]] | ||
| - | [[Category: Bashtannyk-Puhalovich, T | + | [[Category: Bashtannyk-Puhalovich, T A.]] |
| - | [[Category: Bird, C | + | [[Category: Bird, C H.]] |
| - | [[Category: Bird, P | + | [[Category: Bird, P I.]] |
| - | [[Category: Bottomley, S | + | [[Category: Bottomley, S P.]] |
| - | [[Category: Browne, K | + | [[Category: Browne, K A.]] |
| - | [[Category: Buckle, A | + | [[Category: Buckle, A M.]] |
| - | [[Category: Butcher, R | + | [[Category: Butcher, R E.]] |
| - | [[Category: Dunstone, M | + | [[Category: Dunstone, M A.]] |
| - | [[Category: Ellisdon, A | + | [[Category: Ellisdon, A M.]] |
[[Category: Emsley, J.]] | [[Category: Emsley, J.]] | ||
| - | [[Category: Faux, N | + | [[Category: Faux, N G.]] |
| - | [[Category: Hartland, E | + | [[Category: Hartland, E L.]] |
| - | [[Category: Kan, W | + | [[Category: Kan, W T.]] |
| - | [[Category: Law, R | + | [[Category: Law, R H.P.]] |
| - | [[Category: Pearce, M | + | [[Category: Pearce, M C.]] |
| - | [[Category: Pike, R | + | [[Category: Pike, R N.]] |
| - | [[Category: Porter, C | + | [[Category: Porter, C J.]] |
| - | [[Category: Rosado, C | + | [[Category: Rosado, C J.]] |
[[Category: Rossjohn, J.]] | [[Category: Rossjohn, J.]] | ||
| - | [[Category: Smith, A | + | [[Category: Smith, A I.]] |
| - | [[Category: Trapani, J | + | [[Category: Trapani, J A.]] |
[[Category: Ung, K.]] | [[Category: Ung, K.]] | ||
[[Category: Voskoboinik, I.]] | [[Category: Voskoboinik, I.]] | ||
| - | [[Category: Whisstock, J | + | [[Category: Whisstock, J C.]] |
[[Category: Wong, W.]] | [[Category: Wong, W.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: unknown function]] | [[Category: unknown function]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:04 2008'' |
Revision as of 16:41, 21 February 2008
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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, 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.
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 Sep 14;317(5844):1548-51. Epub 2007 Aug 23. PMID:17717151
Page seeded by OCA on Thu Feb 21 18:41:04 2008
Categories: Photorhabdus luminescens subsp. laumondii | Single protein | Baran, K. | Bashtannyk-Puhalovich, T A. | Bird, C H. | Bird, P I. | Bottomley, S P. | Browne, K A. | Buckle, A M. | Butcher, R E. | Dunstone, M A. | Ellisdon, A M. | Emsley, J. | Faux, N G. | Hartland, E L. | Kan, W T. | Law, R H.P. | Pearce, M C. | Pike, R N. | Porter, C J. | Rosado, C J. | Rossjohn, J. | Smith, A I. | Trapani, J A. | Ung, K. | Voskoboinik, I. | Whisstock, J C. | Wong, W. | CA | Toxin | Unknown function
