J
Jurgen Sygusch
Researcher at Université de Montréal
Publications - 71
Citations - 1945
Jurgen Sygusch is an academic researcher from Université de Montréal. The author has contributed to research in topics: Aldolase A & Active site. The author has an hindex of 25, co-authored 71 publications receiving 1739 citations. Previous affiliations of Jurgen Sygusch include Centre national de la recherche scientifique & Paul Sabatier University.
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Journal ArticleDOI
Crystal Structures of DNA-Whirly Complexes and Their Role in Arabidopsis Organelle Genome Repair
Laurent Cappadocia,Alexandre Maréchal,Jean-Sébastien Parent,Étienne Lepage,Jurgen Sygusch,Normand Brisson +5 more
TL;DR: This work shows that plastids and mitochondria can repair DNA double-strand breaks through an error-prone pathway similar to the microhomology-mediated break-induced replication observed in humans, yeast, and bacteria and solves the crystal structures of several Whirly-DNA complexes.
Journal ArticleDOI
Aldolase is essential for energy production and bridging adhesin-actin cytoskeletal interactions during parasite invasion of host cells.
TL;DR: These studies demonstrate that aldolase is not only required for energy production but is also essential for efficient host cell invasion, based on its ability to bridge adhesin-cytoskeleton interactions in the parasite.
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A new family of plant transcription factors displays a novel ssDNA-binding surface.
TL;DR: The crystal structure of p24, the single-stranded DNA (ssDNA) binding subunit of the plant defense transcription factor PBF-2, has been determined to 2.3 Å resolution and the noncrystallographic C4 symmetry arrangement of p 24 subunits is novel for ssDNA binding proteins and may explain the binding specificity of P BF-2.
Journal ArticleDOI
Product binding and role of the C-terminal region in Class I D-fructose 1, 6-bisphosphate aldolase
Nick S. Blom,Jurgen Sygusch +1 more
TL;DR: The structure of fructose 1,6-bisphosphate aldolase shows three distinct modes of product binding that are correlated to the disposition of the C-terminal region and depicts a possible trajectory for product exchange.
Journal ArticleDOI
Structure–Function Profile of MmpL3, the Essential Mycolic Acid Transporter from Mycobacterium tuberculosis
Juan Manuel Belardinelli,Amira Yazidi,Liang Yang,Lucien Fabre,Lucien Fabre,Wei Li,Benoit Jacques,Shiva K. Angala,Isabelle Rouiller,Isabelle Rouiller,Helen I. Zgurskaya,Jurgen Sygusch,Mary Jackson +12 more
TL;DR: The combined genetic, biochemical, and biophysical studies indicate that MmpL3 and CmpL1 are structurally similar to Gram-negative resistance-nodulation and division efflux pumps and that multiresistance to these inhibitors is enabled by conformational changes in MMPL3.