Structure of the type VI secretion system TssK–TssF–TssG baseplate subcomplex revealed by cryo-electron microscopy
暂无分享,去创建一个
F. Dimaio | D. Veesler | C. Cambillau | Young-Jun Park | J. Mougous | Kaitlyn D. Lacourse | Young Jun Park | F. DiMaio | J. D. Mougous
[1] P. Leiman,et al. Contractile injection systems of bacteriophages and related systems , 2018, Molecular microbiology.
[2] C. Cambillau,et al. Towards a complete structural deciphering of Type VI secretion system. , 2018, Current opinion in structural biology.
[3] E. Lindahl,et al. Characterisation of molecular motions in cryo-EM single-particle data by multi-body refinement in RELION , 2018, bioRxiv.
[4] Conrad C. Huang,et al. UCSF ChimeraX: Meeting modern challenges in visualization and analysis , 2018, Protein science : a publication of the Protein Society.
[5] H. Stahlberg,et al. Cryo‐EM reconstruction of Type VI secretion system baseplate and sheath distal end , 2017, The EMBO journal.
[6] C. Cambillau,et al. TssA: The cap protein of the Type VI secretion system tail , 2017, BioEssays : news and reviews in molecular, cellular and developmental biology.
[7] H. Stahlberg,et al. Cryo-EM structure of the extended type VI secretion system sheath–tube complex , 2017, Nature Microbiology.
[8] M. Horn,et al. In situ architecture, function, and evolution of a contractile injection system , 2017, Science.
[9] Marek Basler,et al. The type VI secretion system sheath assembles at the end distal from the membrane anchor , 2017, Nature Communications.
[10] A. Desmyter,et al. Type VI secretion TssK baseplate protein exhibits structural similarity with phage receptor-binding proteins and evolved to bind the membrane complex , 2017, Nature Microbiology.
[11] Frank DiMaio,et al. RosettaES: a sampling strategy enabling automated interpretation of difficult cryo-EM maps , 2017, Nature Methods.
[12] D. Agard,et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy , 2017, Nature Methods.
[13] Davi R. Ortega,et al. In vivo structures of an intact type VI secretion system revealed by electron cryotomography , 2017, bioRxiv.
[14] David J. Fleet,et al. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination , 2017, Nature Methods.
[15] Georgios A. Pavlopoulos,et al. Protein structure determination using metagenome sequence data , 2017, Science.
[16] D. Goodlett,et al. Secreted Effectors Encoded within and outside of the Francisella Pathogenicity Island Promote Intramacrophage Growth. , 2016, Cell host & microbe.
[17] E. Cascales,et al. Molecular Dissection of the Interface between the Type VI Secretion TssM Cytoplasmic Domain and the TssG Baseplate Component. , 2016, Journal of molecular biology.
[18] A. Walls,et al. Crucial steps in the structure determination of a coronavirus spike glycoprotein using cryo‐electron microscopy , 2016, Protein science : a publication of the Protein Society.
[19] H. Stahlberg,et al. Structure of the T4 baseplate and its function in triggering sheath contraction , 2016, Nature.
[20] Frank DiMaio,et al. Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta , 2016, bioRxiv.
[21] M. Rossmann,et al. Role of bacteriophage T4 baseplate in regulating assembly and infection , 2016, Proceedings of the National Academy of Sciences.
[22] C. Cambillau,et al. Priming and polymerization of a bacterial contractile tail structure , 2016, Nature.
[23] David E. Kim,et al. Improved de novo structure prediction in CASP11 by incorporating coevolution information into Rosetta , 2016, Proteins.
[24] E. Cascales,et al. The Type VI Secretion TssEFGK-VgrG Phage-Like Baseplate Is Recruited to the TssJLM Membrane Complex via Multiple Contacts and Serves As Assembly Platform for Tail Tube/Sheath Polymerization , 2015, PLoS genetics.
[25] David E. Kim,et al. Large-scale determination of previously unsolved protein structures using evolutionary information , 2015, eLife.
[26] A. Desmyter,et al. Biogenesis and structure of a type VI secretion membrane core complex , 2015, Nature.
[27] Kai Zhang,et al. Gctf: Real-time CTF determination and correction , 2015, bioRxiv.
[28] Z. Zhou,et al. Atomic structures of a bactericidal contractile nanotube in its pre- and postcontraction states , 2015, Nature Structural &Molecular Biology.
[29] Z. Zhou,et al. Atomic Structure of T6SS Reveals Interlaced Array Essential to Function , 2015, Cell.
[30] David Baker,et al. Structure of the Type VI Secretion System Contractile Sheath , 2015, Cell.
[31] Matthias J. Brunner,et al. Atomic accuracy models from 4.5 Å cryo-electron microscopy data with density-guided iterative local refinement , 2015, Nature Methods.
[32] A. Prescott,et al. Biochemical analysis of TssK, a core component of the bacterial Type VI secretion system, reveals distinct oligomeric states of TssK and identifies a TssK–TssFG subcomplex , 2014, The Biochemical journal.
[33] R. Henderson,et al. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy☆ , 2013, Ultramicroscopy.
[34] A. Steven,et al. One number does not fit all: mapping local variations in resolution in cryo-EM reconstructions. , 2013, Journal of structural biology.
[35] David Baker,et al. High-resolution comparative modeling with RosettaCM. , 2013, Structure.
[36] J. Mekalanos,et al. PAAR-repeat proteins sharpen and diversify the Type VI secretion system spike , 2013, Nature.
[37] C. Cambillau,et al. TssK Is a Trimeric Cytoplasmic Protein Interacting with Components of Both Phage-like and Membrane Anchoring Complexes of the Type VI Secretion System* , 2013, The Journal of Biological Chemistry.
[38] Thomas A. Hopf,et al. Protein structure prediction from sequence variation , 2012, Nature Biotechnology.
[39] Shaoxia Chen,et al. Prevention of overfitting in cryo-EM structure determination , 2012, Nature Methods.
[40] D. Veesler,et al. Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism , 2012, Proceedings of the National Academy of Sciences.
[41] C. Cambillau,et al. Structural biology of type VI secretion systems , 2012, Philosophical Transactions of the Royal Society B: Biological Sciences.
[42] G. Jensen,et al. Type VI secretion requires a dynamic contractile phage tail-like structure , 2012, Nature.
[43] Christian Cambillau,et al. A Common Evolutionary Origin for Tailed-Bacteriophage Functional Modules and Bacterial Machineries , 2011, Microbiology and Molecular Reviews.
[44] J. Rubinstein,et al. Phages have adapted the same protein fold to fulfill multiple functions in virion assembly , 2010, Proceedings of the National Academy of Sciences.
[45] G. Sciara,et al. Structure of lactococcal phage p2 baseplate and its mechanism of activation , 2010, Proceedings of the National Academy of Sciences.
[46] P. Emsley,et al. Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.
[47] D. Goodlett,et al. A type VI secretion system of Pseudomonas aeruginosa targets a toxin to bacteria. , 2010, Cell host & microbe.
[48] M Radermacher,et al. DoG Picker and TiltPicker: software tools to facilitate particle selection in single particle electron microscopy. , 2009, Journal of structural biology.
[49] Christopher Irving,et al. Appion: an integrated, database-driven pipeline to facilitate EM image processing. , 2009, Journal of structural biology.
[50] A. Davidson,et al. The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system , 2009, Proceedings of the National Academy of Sciences.
[51] J. M. Sauder,et al. Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin , 2009, Proceedings of the National Academy of Sciences.
[52] E. Cascales. The type VI secretion toolkit , 2008, EMBO reports.
[53] G. Waksman,et al. Identification, structure and mode of action of a new regulator of the Helicobacter pylori HP0525 ATPase , 2007, The EMBO journal.
[54] Andrew T. Revel,et al. Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin , 2007, Proceedings of the National Academy of Sciences.
[55] K. Henrick,et al. Inference of macromolecular assemblies from crystalline state. , 2007, Journal of molecular biology.
[56] Stephen Lory,et al. A Virulence Locus of Pseudomonas aeruginosa Encodes a Protein Secretion Apparatus , 2006, Science.
[57] W. Nelson,et al. Identification of a conserved bacterial protein secretion system in Vibrio cholerae using the Dictyostelium host model system , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[58] Anchi Cheng,et al. Automated molecular microscopy: the new Leginon system. , 2005, Journal of structural biology.
[59] Michael G. Rossmann,et al. Three-Dimensional Rearrangement of Proteins in the Tail of Bacteriophage T4 on Infection of Its Host , 2004, Cell.
[60] R. Henderson,et al. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. , 2003, Journal of molecular biology.
[61] Fumio Arisaka,et al. Structure of the cell-puncturing device of bacteriophage T4 , 2002, Nature.
[62] D. Ladant,et al. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[63] Conrad C. Huang,et al. Visualizing density maps with UCSF Chimera. , 2007, Journal of structural biology.