Bibliography
De Colibus, L., Sonnen, A. F.-P., Morris, K. J., Siebert, C. A., Abrusci, P., Plitzko, J., Hodnik, V., Leippe, M., Volpi, E., Anderluh, G., & Gilbert, R. J. C. (2012). Structures of Lysenin Reveal a Shared Evolutionary Origin for Pore-Forming Proteins And Its Mode of Sphingomyelin Recognition. Structure, 20(9), 1498â1507.
Authors
11
- Luigi De Colibus (first)
- Andreas F.-P. Sonnen (additional)
- Keith J. Morris (additional)
- C. Alistair Siebert (additional)
- Patrizia Abrusci (additional)
- Jürgen Plitzko (additional)
- Vesna Hodnik (additional)
- Matthias Leippe (additional)
- Emanuela Volpi (additional)
- Gregor Anderluh (additional)
- Robert J.C. Gilbert (additional)
References
59
Referenced
86
10.1107/S0907444995008754
/ Acta Crystallogr. D Biol. Crystallogr. / Methods used in the structure determination of bovine mitochondrial F1 ATPase by Abrahams (1996)10.1016/j.jmb.2008.12.002
/ J. Mol. Biol. / Crystal structure of the parasporin-2 Bacillus thuringiensis toxin that recognizes cancer cells by Akiba (2009)10.1016/j.chom.2007.12.007
/ Cell Host Microbe / Host cell traversal is important for progression of the malaria parasite through the dermis to the liver by Amino (2008)10.1016/j.ab.2005.06.013
/ Anal. Biochem. / Properties of nonfused liposomes immobilized on an L1 Biacore chip and their permeabilization by a eukaryotic pore-forming toxin by Anderluh (2005)10.1016/j.tibs.2008.07.004
/ Trends Biochem. Sci. / Disparate proteins use similar architectures to damage membranes by Anderluh (2008)10.1074/jbc.M708747200
/ J. Biol. Chem. / Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin by Bakrac (2008)10.1107/S0907444904016427
/ Acta Crystallogr. D Biol. Crystallogr. / Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT by Blanc (2004)10.1016/j.dci.2005.09.002
/ Dev. Comp. Immunol. / Dissection of the mechanisms of cytolytic and antibacterial activity of lysenin, a defence protein of the annelid Eisenia fetida by Bruhn (2006)10.1107/S0907444998003254
/ Acta Crystallogr. D Biol. Crystallogr. / Crystallography & NMR system: A new software suite for macromolecular structure determination by Brünger (1998)10.1002/jcc.20290
/ J. Comput. Chem. / The Amber biomolecular simulation programs by Case (2005)10.1107/S0907444994003112
/ Acta Crystallogr. D Biol. Crystallogr. / The CCP4 suite: programs for protein crystallography (1994)10.1107/S0907444909042073
/ Acta Crystallogr. D Biol. Crystallogr. / MolProbity: all-atom structure validation for macromolecular crystallography by Chen (2010)10.1038/nsmb804
/ Nat. Struct. Mol. Biol. / Clostridium perfringens epsilon-toxin shows structural similarity to the pore-forming toxin aerolysin by Cole (2004)10.1038/nature10742
/ Nature / Molecular recognition of a single sphingolipid species by a protein’s transmembrane domain by Contreras (2012)10.1007/978-1-4615-1291-2_15
/ Adv. Exp. Med. Biol. / Annelid humoral immunity: cell lysis in earthworms by Cooper (2001){'key': '10.1016/j.str.2012.06.011_bib16', 'first-page': '34', 'article-title': 'DM: an automated procedure for phase improvement by density modification', 'volume': '31', 'author': 'Cowtan', 'year': '1994', 'journal-title': 'Joint CCP4 ESF-EACBM Newsl Protein Crystallogr'}
/ Joint CCP4 ESF-EACBM Newsl Protein Crystallogr / DM: an automated procedure for phase improvement by density modification by Cowtan (1994)10.1107/S0907444906022116
/ Acta Crystallogr. D Biol. Crystallogr. / The Buccaneer software for automated model building. 1. Tracing protein chains by Cowtan (2006)10.1006/jsbi.1996.0003
/ J. Struct. Biol. / MRC image processing programs by Crowther (1996)10.1016/S0076-6879(97)76073-7
/ Methods Enzymol. / Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods by de la Fortelle (1997)10.1107/S0907444904019158
/ Acta Crystallogr. D Biol. Crystallogr. / Coot: model-building tools for molecular graphics by Emsley (2004)10.1063/1.470117
/ J. Chem. Phys. / A smooth particle mesh Ewald method by Essmann (1995)10.1107/S0907444905036693
/ Acta Crystallogr. D Biol. Crystallogr. / Scaling and assessment of data quality by Evans (2006)10.1093/sysbio/46.1.101
/ Syst. Biol. / An alternating least squares approach to inferring phylogenies from pairwise distances by Felsenstein (1997)10.1107/S0567739478001114
/ Acta Crystallogr. A / On the treatment of negative intensity observations by French (1978)10.1007/978-1-4419-6741-1_1
/ Adv. Exp. Med. Biol. / An overview of sphingolipid metabolism: from synthesis to breakdown by Gault (2010)10.1016/j.jsb.2006.07.020
/ J. Struct. Biol. / 2dx—user-friendly image processing for 2D crystals by Gipson (2007)10.1016/j.str.2005.04.019
/ Structure / Inactivation and activity of cholesterol-dependent cytolysins: what structural studies tell us by Gilbert (2005)10.1007/978-1-4419-6327-7_5
/ Adv. Exp. Med. Biol. / Cholesterol-dependent cytolysins by Gilbert (2010)10.1038/nature10370
/ Nature / Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2 by Hansen (2011)10.1038/emboj.2010.68
/ EMBO J. / Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals by Hite (2010)10.1093/nar/gkq366
/ Nucleic Acids Res. / Dali server: conservation mapping in 3D by Holm (2010){'key': '10.1016/j.str.2012.06.011_bib32', 'first-page': '203', 'article-title': 'Imaging lipid membrane domains with lipid-specific probes', 'volume': '580', 'author': 'Hullin-Matsuda', 'year': '2009', 'journal-title': 'Methods Mol. Biol.'}
/ Methods Mol. Biol. / Imaging lipid membrane domains with lipid-specific probes by Hullin-Matsuda (2009)10.1371/journal.ppat.1002135
/ PLoS Pathog. / Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin by Iacovache (2011)10.1111/j.1447-073x.2004.00086.x
/ Anat. Sci. Int. / Lysenin: a new tool for investigating membrane lipid organization by Ishitsuka (2004)10.1107/S0021889893005588
/ J. Appl. Cryst. / Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants by Kabsch (1993)10.1021/bi049561j
/ Biochemistry / Recognition of sphingomyelin by lysenin and lysenin-related proteins by Kiyokawa (2004)10.1074/jbc.M502244200
/ J. Biol. Chem. / Spatial and functional heterogeneity of sphingolipid-rich membrane domains by Kiyokawa (2005)10.1080/09687860600995540
/ Mol. Membr. Biol. / Lysenin-His, a sphingomyelin-recognizing toxin, requires tryptophan 20 for cation-selective channel assembly but not for membrane binding by Kwiatkowska (2007)10.1016/j.str.2003.09.019
/ Structure / Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation by Mancheño (2003)10.1074/jbc.M413933200
/ J. Biol. Chem. / Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars by Mancheño (2005)10.1107/S0021889807021206
/ J. Appl. Cryst. / Phaser crystallographic software by McCoy (2007)10.1038/nature08026
/ Nature / The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism by Mueller (2009)10.1038/5821
/ Nat. Struct. Biol. / Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel by Olson (1999)10.1107/S0021889805038987
/ J. Appl. Cryst. / TLSMD web server for the generation of multi-group TLS models by Painter (2006)10.1038/367292a0
/ Nature / Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states by Parker (1994)10.1038/362219a0
/ Nature / Crystal structure of globular domain of histone H5 and its implications for nucleosome binding by Ramakrishnan (1993)10.1016/S0969-2126(02)00896-1
/ Structure / Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins by Riffel (2002)10.1111/j.1462-5822.2008.01191.x
/ Cell. Microbiol. / The MACPF/CDC family of pore-forming toxins by Rosado (2008)10.1002/ijc.2910190505
/ Int. J. Cancer / Characterization of EBV-genome negative “null” and “T” cell lines derived from children with acute lymphoblastic leukemia and leukemic transformed non-Hodgkin lymphoma by Schneider (1977)10.1107/S0907444902011678
/ Acta Crystallogr. D Biol. Crystallogr. / Substructure solution with SHELXD by Schneider (2002)10.1128/IAI.68.10.5546-5551.2000
/ Infect. Immun. / Clostridium perfringens beta-toxin forms potential-dependent, cation-selective channels in lipid bilayers by Shatursky (2000)10.1126/science.274.5294.1859
/ Science / Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore by Song (1996)10.1016/0022-2836(79)90416-9
/ J. Mol. Biol. / Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A by Stuart (1979)10.1371/journal.pone.0020349
/ PLoS ONE / Extending the aerolysin family: from bacteria to vertebrates by Szczesny (2011)10.1016/j.cell.2005.02.033
/ Cell / Structural basis of pore formation by the bacterial toxin pneumolysin by Tilley (2005)10.1107/S0907444901012409
/ Acta Crystallogr. D Biol. Crystallogr. / Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps by Vagin (2001)10.1006/jmbi.1994.1445
/ J. Mol. Biol. / Analysis of electron microscope images and electron diffraction patterns of thin crystals of phi 29 connectors in ice by Valpuesta (1994)10.1107/S0907444905007808
/ Acta Crystallogr. D Biol. Crystallogr. / A procedure for setting up high-throughput nanolitre crystallization experiments. Crystallization workflow for initial screening, automated storage, imaging and optimization by Walter (2005)10.1074/jbc.M213209200
/ J. Biol. Chem. / Oligomerization and pore formation of a sphingomyelin-specific toxin, lysenin by Yamaji-Hasegawa (2003)
@article{De_Colibus_2012, title={Structures of Lysenin Reveal a Shared Evolutionary Origin for Pore-Forming Proteins And Its Mode of Sphingomyelin Recognition}, volume={20}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/j.str.2012.06.011}, DOI={10.1016/j.str.2012.06.011}, number={9}, journal={Structure}, publisher={Elsevier BV}, author={De Colibus, Luigi and Sonnen, Andreas F.-P. and Morris, Keith J. and Siebert, C. Alistair and Abrusci, Patrizia and Plitzko, Jürgen and Hodnik, Vesna and Leippe, Matthias and Volpi, Emanuela and Anderluh, Gregor and Gilbert, Robert J.C.}, year={2012}, month=sep, pages={1498–1507} }