Výsledky vyhledávání - "chemistry [Bacterial Proteins]"

A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover

Autor: Giambattista Guaitoli, Frank Sobott, Rodrigo Gallardo, Arjan Kortholt, Albert Konijnenberg, Egon Deyaert, Margaux Leemans, Lina Wauters, Henderikus Pots, Peter J.M. van Haastert, Rouslan G. Efremov, Arsen Petrovic, Christian Johannes Gloeckner, Susanne Terheyden, Laura M Nederveen-Schippers, Panagiotis S Athanasopoulos, Wim Versées

Publikováno v: Nature Communications 8(1), 1008 (2017). doi:10.1038/s41467-017-01103-4
Nature Communications, 8(1):1008, 1-12. Nature Publishing Group
'Nature Communications ', vol: 8, pages: 1008-1-1008-12 (2017)
Nature Communications
Nature communications
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)

Mutations in LRRK2 are a common cause of genetic Parkinson’s disease (PD). LRRK2 is a multi-domain Roco protein, harbouring kinase and GTPase activity. In analogy with a bacterial homologue, LRRK2 was proposed to act as a GTPase activated by dimeri

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Cold denaturation of a protein dimer monitored at atomic resolution

Autor: Mariusz Jaremko, Markus Zweckstetter, Stefan Becker, Charles D. Schwieters, Hai-Young Kim, Min-Kyu Cho, Karin Giller, Łukasz Jaremko

Publikováno v: Nature chemical biology 9(4), 264-270 (2013). doi:10.1038/nchembio.1181
Nature Chemical Biology

Protein folding and unfolding are crucial for a range of biological phenomena and human diseases. Defining the pathways of protein folding and unfolding is crucial for understanding the origins of a range of biological phenomena and human diseases. H

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https://doi.org/10.1038/nchembio.1181

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Ligand Binding Induces an Ammonia Channel in 2-Amino-2-desoxyisochorismate (ADIC) Synthase PhzE

Autor: Manfred Roessle, Linda S. Thomashow, Wulf Blankenfeldt, Dmitri V. Mavrodi, Qi Ang Li

Publikováno v: The journal of biological chemistry 286, 18213-18221 (2011). doi:10.1074/jbc.M110.183418

PhzE utilizes chorismate and glutamine to synthesize 2-amino-2-desoxyisochorismate (ADIC) in the first step of phenazine biosynthesis. The PhzE monomer contains both a chorismate-converting menaquinone, siderophore, tryptophan biosynthesis (MST) and

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https://doi.org/10.1074/jbc.m110.183418

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Structural and Thermodynamic Characterization of Metal Ion Binding in Streptococcus suis Dpr

Autor: Anastassios C. Papageorgiou, Teemu Haikarainen, Sauli Haataja, Angelos Thanassoulas, George Nounesis, Philemon Stavros

Publikováno v: Journal of molecular biology 405, 448-60 (2011). doi:10.1016/j.jmb.2010.10.058

The use of protein cages for the creation of novel inorganic nanomaterials has attracted considerable attention in recent years. Ferritins are among the most commonly used protein cages in nanoscience. Accordingly, the binding of various metals to fe

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https://doi.org/10.1016/j.jmb.2010.10.058

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A structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3d

Autor: Alexey Zozulya, Jean M. H. van den Elsen, D. I. Svergun, Susan J. Crennell, Abhishek Upadhyay, Julia D. Mackay, Elizabeth A. Clark, Stefan Bagby

Publikováno v: Molecular Immunology
Molecular immunology 48, 452-462 (2011). doi:10.1016/j.molimm.2010.09.017

The structure of the complement-binding domain of Staphylococcus aureus protein Sbi (Sbi-IV) in complex with ligand C3d is presented. The 1.7 A resolution structure reveals the molecular details of the recognition of thioester-containing fragment C3d

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Structural and Kinetic Studies on Native Intermediates and an Intermediate Analogue in Benzoylformate Decarboxylase Reveal a Least Motion Mechanism with an Unprecedented Short-Lived Predecarboxylation Intermediate

Autor: Hans Bartunik, Kai Tittmann, Andreas Liese, Ralph Golbik, Marco Berheide, Danilo Meyer, Marc Bruning

Publikováno v: Biochemistry 48, 3258-3268 (2009). doi:10.1021/bi801957d

Biochemistry 48, 3258-3268 (2009). doi:10.1021/bi801957d
The thiamin diphosphate- (ThDP-) dependent enzyme benzoylformate decarboxylase (BFDC) catalyzes the nonoxidative decarboxylation of benzoylformic acid to benzaldehyde and carbon dioxide. T

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https://doi.org/10.1021/bi801957d

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X-ray and Neutron Small-Angle Scattering Analysis of the Complex Formed by the Met Receptor and the Listeria monocytogenes Invasion Protein InlB

Autor: Dirk W. Heinz, Hartmut H. Niemann, Maxim V. Petoukhov, Martine Moulin, Dmitri I. Svergun, Ermanno Gherardi, Michael Härtlein, Peter Timmins

Publikováno v: Journal of molecular biology 377, 489-500 (2008). doi:10.1016/j.jmb.2008.01.027
Journal of Molecular Biology; Vol 377

The Listeria monocytogenes surface protein InIB binds to the extracellular domain of the human receptor tyrosine kinase Met, the product of the c-met proto-oncogene. InlB binding activates the Met receptor, leading to uptake of Listeria into normally

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https://doi.org/10.1016/j.jmb.2008.01.027

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Structure of the mammalian TSPO/PBR protein

Autor: Mariusz Jaremko, Stefan Becker, Garima Jaipuria, Markus Zweckstetter, Łukasz Jaremko

Publikováno v: Biochemical Society Transactions
Biochemical Society transactions 43(4), 566-571 (2015). doi:10.1042/BST20150029

The 3D structure of the 18-kDa transmembrane (TM) protein TSPO (translocator protein)/PBR (peripheral benzodiazepine receptor), which contains a binding site for benzodiazepines, is important to better understand its function and regulation by endoge

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https://pubmed.ncbi.nlm.nih.gov/26551694

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Identification of Basic Amino Acid Residues Important for Citrate Binding by the Periplasmic Receptor Domain of the Sensor Kinase CitA

Autor: Stefan Reinelt, Leonardo Scapozza, Sibylle Kaspar, Tanja Gerharz, Michael Bott

Publikováno v: Biochemistry 42, 5917-5924 (2003). doi:10.1021/bi0340595

The sensor kinase CitA and the response regulator CitB of Klebsiella pneumoniae form the paradigm of a subfamily of bacterial two-component regulatory systems that are capable of sensing tri- or dicarboxylates in the environment and then induce trans

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https://doi.org/10.1021/bi0340595

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