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Crystal structure of a Baeyer-Villiger monooxygenase.
- E. Malito, A. Alfieri, M. Fraaije, A. Mattevi
- Chemistry, BiologyProceedings of the National Academy of Sciences…
- 7 September 2004
The structural studies highlight the functional complexity of this class of flavoenzymes, which coordinate the binding of three substrates in proximity of the flavin cofactor with formation of two distinct catalytic intermediates.
Amyloid β-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin
Structural and biochemical insights into cryptidases provide potential therapeutic strategies for the control of Aβ clearance and suggest a role for presequence peptidase in the degradation of mitochondrial Aβ.
Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis.
Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase
- A. Alfieri, E. Malito, R. Orrú, M. Fraaije, A. Mattevi
- BiologyProceedings of the National Academy of Sciences
- 6 May 2008
Localization of mutations in human FMO3 that are known to cause trimethylaminuria (fish-odor syndrome) in the elucidated FMO structure provides a structural explanation for their biological effects.
Self-assembling protein nanoparticles in the design of vaccines
Structure of Substrate-free Human Insulin-degrading Enzyme (IDE) and Biophysical Analysis of ATP-induced Conformational Switch of IDE*
The interaction between ATP and activating mutations rendered IDE less sensitive to ATP activation, suggesting that ATP might facilitate the transition from the closed state to the open conformation, and ATP induced an increase in hydrodynamic radius, a shift in electrophoretic mobility, and changes in secondary structure.
Cellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracis*
It is shown that the apical application of ALO decreases the barrier function of human polarized epithelial cells as well as increases intracellular calcium and the internalization of the tight junction protein occludin.
Structural basis for lack of toxicity of the diphtheria toxin mutant CRM197
- E. Malito, B. Bursulaya, G. Spraggon
- Biology, ChemistryProceedings of the National Academy of Sciences
- 19 March 2012
The crystal structures of the full-length nucleotide-free CRM197 and ofCRM197 in complex with the NAD hydrolysis product nicotinamide (NCA) are determined and show for the first time that the overall fold of CRM 197 and DT are nearly identical and that the striking functional difference between the two proteins can be explained by a flexible active-site loop that covers the NAD binding pocket.
Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine.
Structural basis for potent antibody-mediated neutralization of human cytomegalovirus
Crystal structures of neutralizing antibodies bound to the HCMV pentameric complex (Pentamer), a key determinant of viral entry, are reported and structural and functional studies identify potential entry receptor–binding sites on Pentamer as well as other functional sites that may serve as targets for vaccine development and antibody and small-molecule therapeutics.