Výsledky vyhledávání - "MESH: Thermotoga maritima"

Overproduction, purification, crystallization and preliminary X-ray analysis of the peroxiredoxin domain of a larger natural hybrid protein fromThermotoga maritima

Autor: Nicolas Rouhier, Jean-Pierre Jacquot, Carole Barbey, Ahmed Haouz, Alda Navaza

Publikováno v: Acta crystallographica Section F : Structural biology communications [2014-...]
Acta crystallographica Section F : Structural biology communications [2014-..], 2008, 64 (1), pp.29-31. ⟨10.1107/S1744309107064391⟩
Acta crystallographica. Section F, Structural biology communications
Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd, 2008, 64 (1), pp.29-31. ⟨10.1107/S1744309107064391⟩

International audience; Thermotoga maritima contains a natural hybrid protein constituted of two moieties: a peroxiredoxin domain at the N-terminus and a nitroreductase domain at the C-terminus. The peroxiredoxin (Prx) domain has been overproduced an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b348df9751079eb89a24f550fcf2fed
https://doi.org/10.1107/s1744309107064391

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MreB and MurG as scaffolds for the cytoplasmic steps of peptidoglycan biosynthesis

Autor: Favini-Stabile, Sandy, Contreras-Martel, Carlos, Thielens, Nicole, Dessen, Andréa

Publikováno v: Environmental Microbiology
Environmental Microbiology, Society for Applied Microbiology and Wiley-Blackwell, 2013, 15 (12), pp.3218-28. ⟨10.1111/1462-2920.12171⟩
Environmental Microbiology, 2013, 15 (12), pp.3218-28. ⟨10.1111/1462-2920.12171⟩

International audience; Peptidoglycan is a major determinant of cell shape in bacteria, and its biosynthesis involves the concerted action of cytoplasmic, membrane-associated and periplasmic enzymes. Within the cytoplasm, Mur enzymes catalyse the fir

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::cac22dd3f4516bb4c05cadba2d254cb0
https://hal.univ-grenoble-alpes.fr/hal-01321663

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Ultrafast real-time visualization of active site flexibility of flavoenzyme thymidylate synthase ThyX

Autor: Hannu Myllykallio, Marten H. Vos, Sergey P. Laptenok, Ursula Liebl, Latifa Bouzhir-Sima, Jean-Christophe Lambry

In many bacteria the flavoenzyme thymidylate synthase ThyX produces the DNA nucleotide deoxythymidine monophosphate from dUMP, using methylenetetrahydrofolate as carbon donor and NADPH as hydride donor. Because all three substrates bind in close prox

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3d053cb02a63183bcee170f785db079
https://hal-polytechnique.archives-ouvertes.fr/hal-00942352

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X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters

Autor: Roman Rohac, Lydie Martin, Yvain Nicolet, Juan-Carlos Fontecilla-Camps

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (18), pp.7188-7192. ⟨10.1073/pnas.1302388110⟩
Proceedings of the National Academy of Sciences of the United States of America, 2013, 110 (18), pp.7188-7192. ⟨10.1073/pnas.1302388110⟩

Fe 4 S 4 clusters are very common versatile prosthetic groups in proteins. Their redox property of being sensitive to O 2 -induced oxidative damage is, for instance, used by the cell to sense oxygen levels and switch between aerobic and anaerobic met

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bddbe2b878fd6c0c492327263a7d6ad9
https://hal.archives-ouvertes.fr/hal-01664850

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Mutagenesis via IS transposition in Deinococcus radiodurans

Autor: Pascale Servant, Samuel Mennecier, Suzanne Sommer, Adriana Bailone, Geneviève Coste

Publikováno v: Molecular Microbiology
Molecular Microbiology, Wiley, 2006, 59, pp.317-25
Molecular Microbiology, Wiley, 2006, 59 (1), pp.317-25. ⟨10.1111/j.1365-2958.2005.04936.x⟩

Analysis of the complete genome indicates that insertion sequences (ISs) are abundant in the radio-resistant bacterium Deinococcus radiodurans. By developing a forward mutagenesis assay to detect any inactivation events in D. radiodurans, we found th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1a8573428b8aa08493f873d36ae48aa
https://hal.archives-ouvertes.fr/hal-00079728

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