M
Mischa Machius
Researcher at University of Texas Southwestern Medical Center
Publications - 80
Citations - 7050
Mischa Machius is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Binding site & Protein structure. The author has an hindex of 43, co-authored 78 publications receiving 6558 citations. Previous affiliations of Mischa Machius include University of North Carolina at Chapel Hill & Max Planck Society.
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Journal ArticleDOI
Three-dimensional structure of the complexin/SNARE complex.
Xiaocheng Chen,Diana R. Tomchick,Evguenii Kovrigin,Demet Araç,Mischa Machius,Thomas C. Südhof,Josep Rizo +6 more
TL;DR: The results suggest that complexin stabilizes the fully assembled SNARE complex as a key step that enables the exquisitely high speed of Ca(2+)-evoked neurotransmitter release.
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Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
Takanori Otomo,Diana R. Tomchick,Chinatsu Otomo,Sanjay C. Panchal,Mischa Machius,Michael K. Rosen +5 more
TL;DR: The crystal structure of the yeast Bni1p FH2 domain in complex with tetramethylrhodamine–actin is reported, showing each of the two structural units in the FH1 dimer binds two actins in an orientation similar to that in an actin filament, suggesting this structure could function as a filament nucleus.
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Pivotal role of water in the mechanism of P450BM-3.
TL;DR: The crystal structure of a complex between the bacterial P450BM-3 and the novel substrate N-palmitoylglycine at a resolution of 1.65 A is described, which reveals previously unrecognizable features of active site reorganization upon substrate binding.
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Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution.
TL;DR: The three-dimensional structure of Bacillus licheniformis alpha-amylase (BLA) has been determined by multiple isomorphous replacement in a crystal of space group P4(3)2(1)2 (a = b = 119.6 A, c = 85.4 A) as discussed by the authors.
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Structural Basis for Corest-Dependent Demethylation of Nucleosomes by the Human Lsd1 Histone Demethylase
Maojun Yang,Christian B. Gocke,Xuelian Luo,Dominika Borek,Diana R. Tomchick,Mischa Machius,Zbyszek Otwinowski,Hongtao Yu +7 more
TL;DR: The crystal structure of the LSD1-CoREST complex forms an elongated structure with a long stalk connecting the catalytic domain of LSD1 and the CoREST SANT2 domain, suggesting its bivalent binding to nucleosomes, allowing efficient H3-K4 demethylation.