Výsledky vyhledávání - "Laura M. van Staalduinen"

Akademický článek

Post-translational hydroxylation by 2OG/Fe(II)-dependent oxygenases as a novel regulatory mechanism in bacteria

Autor: Laura M van Staalduinen, Zongchao eJia

Publikováno v: Frontiers in Microbiology, Vol 5 (2015)

Protein hydroxylation has been well-studied in eukaryotic systems. The structural importance of hydroxylation of specific proline and lysine residues during collagen biosynthesis is well established while, recently, key roles for post-translational h

Externí odkaz: https://doaj.org/article/5bbd05f6db97428abc9f3dc71145b0bc

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Going Platinum to the Tune of a Remarkable Guanine Quadruplex Binder: Solution‐ and Solid‐State Investigations

Autor: Alana M. M. Rangaswamy, Zongchao Jia, Caitlin E. Miron, Laura M. van Staalduinen, Mickey Chen, Yushi Liang, Anne Petitjean, Jean-Louis Mergny

Publikováno v: Angewandte Chemie International Edition
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2020, Online ahead of print. ⟨10.1002/anie.202012520⟩
Angewandte Chemie International Edition, 2020, Online ahead of print. ⟨10.1002/anie.202012520⟩

International audience; Guanine quadruplex recognition has gained increasing attention, inspired by the growing awareness of the key roles played by these non-canonical nucleic acid architectures in cellular regulatory processes. We report here the s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25a9718f4deff99e8008f6ac17534b62
https://www.hal.inserm.fr/inserm-02976985

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Structure and Functional Analysis of YcfD, a Novel 2-Oxoglutarate/Fe2+-Dependent Oxygenase Involved in Translational Regulation in Escherichia coli

Autor: Stefanie K. Novakowski, Zongchao Jia, Laura M. van Staalduinen

Publikováno v: Journal of Molecular Biology. 426:1898-1910

The 2-oxoglutarate (2OG)/Fe2 +-dependent oxygenases (2OG oxygenases) are a large family of proteins that share a similar overall three-dimensional structure and catalyze a diverse array of oxidation reactions. The Jumonji C (JmjC)-domain-containing p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a77fde1f2ee2467f597d2823d15f265a
https://doi.org/10.1016/j.jmb.2014.02.008

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Crystal structure of PhnZ in complex with substrate reveals a di-iron oxygenase mechanism for catabolism of organophosphonates

Autor: Jacqueline Séguin, Katharina Schiessl, David L. Zechel, Friedrich Hammerschmidt, Laura M. van Staalduinen, Fern R. McSorley, Peter B. Wyatt, Zongchao Jia

Publikováno v: Proceedings of the National Academy of Sciences. 111:5171-5176

The enzymes PhnY and PhnZ comprise an oxidative catabolic pathway that enables marine bacteria to use 2-aminoethylphosphonic acid as a source of inorganic phosphate. PhnZ is notable for catalyzing the oxidative cleavage of a carbon-phosphorus bond us

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e2c54d9d963dfd70c9ff45b3f3f96bc
https://doi.org/10.1073/pnas.1320039111

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Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) α-kinase domain apoenzyme reveals a novel autoinhibited conformation

Autor: Yidai Yang, Laura M. van Staalduinen, Graham P. Côté, Linda Liu, Scott W. Crawley, Zongchao Jia, Qilu Ye, Stephanie Brennan

Publikováno v: Scientific Reports

The α-kinases are a family of a typical protein kinases present in organisms ranging from protozoa to mammals. Here we report an autoinhibited conformation for the α-kinase domain of Dictyostelium myosin-II heavy chain kinase A (MHCK-A) in which nu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b7be3e8a17ca0ad0c9efec2a574a71b
https://doi.org/10.1038/srep26634

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Crystal Structure of PhnH: an Essential Component of Carbon-Phosphorus Lyase in Escherichia coli

Autor: Melanie A. Adams, Yan Luo, Bjarne Hove-Jensen, David L. Zechel, Shu-Mei He, Laura M. van Staalduinen, Zongchao Jia

Publikováno v: Journal of Bacteriology. 190:1072-1083

Organophosphonates are reduced forms of phosphorous that are characterized by the presence of a stable carbon-phosphorus (C-P) bond, which resists chemical hydrolysis, thermal decomposition, and photolysis. The chemically inert nature of the C-P bond

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56faa0c55c87b8b76564b5fadcd65402
https://doi.org/10.1128/jb.01274-07

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Structure-based annotation of a novel sugar isomerase from the pathogenic E. coli O157:H7

Autor: Chang-Su Park, Zongchao Jia, Laura M. van Staalduinen, Deok-Kun Oh, Melanie A. Adams-Cioaba, Soo-Jin Yeom

Publikováno v: Journal of molecular biology. 401(5)

Prokaryotes can use a variety of sugars as carbon sources in order to provide a selective survival advantage. The gene z5688 found in the pathogenic Escherichia coli O157:H7 encodes a "hypothetical" protein of unknown function. Sequence analysis iden

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3257c775b16fa1bfdf732717e96a7ba9
https://pubmed.ncbi.nlm.nih.gov/20615418

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Expression, purification and preliminary X-ray diffraction studies of RebC

Autor: Katherine Groom, Anupam Bhattacharya, Zongchao Jia, Laura M. van Staalduinen, David L. Zechel

Publikováno v: Acta crystallographica. Section F, Structural biology and crystallization communications. 63(Pt 11)

The flavin-dependent monooxygenase RebC is a key enzyme in the biosynthesis of the indolocarbazole rebeccamycin. The synthesis of rebeccamycin is of great interest as it has been shown to be a natural antitumour agent. The enzyme has been recombinant

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ab8c269cbbb9fe800ac4ca6217efd00
https://pubmed.ncbi.nlm.nih.gov/18007056

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Structure of PhnZ reveals a novel oxygenase mechanism for C-P bond cleavage

Autor: Laura M. van Staalduinen, Fern R. McSorley, Zongchao Jia, David L. Zechel

Publikováno v: Acta Crystallographica Section A Foundations and Advances. 70:C1281-C1281

Inorganic phosphate is an essential component of many biological molecules and processes including cellular signaling, generation of metabolic energy, DNA and RNA, and membrane phospholipids. Organophosphonates, which contain a highly stable carbon-p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0c408604c1a6fda197fcf248e5f741ce
https://doi.org/10.1107/s205327331408718x

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Structure and Functional Analysis of a Ribosomal Oxygenase

Autor: Stefanie K. Novakowski, Zongchao Jia, Laura M. van Staalduinen

Publikováno v: Acta Crystallographica Section A Foundations and Advances. 70:C1408-C1408

The 2-oxoglutarate/Fe(II)-dependent oxygenases (2OG oxygenases) are a large family of proteins that share a similar overall three-dimensional structure and catalyze a diverse array of oxidation reactions. The Jumonji C (JmjC)-domain containing protei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9d855f849001ba5c953dd74ff396bb35
https://doi.org/10.1107/s205327331408591x

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