Towards a structural comprehension of bacterial type VI secretion systems: characterization of the TssJ-TssM complex of an Escherichia coli pathovar.

Autor: Catarina Felisberto-Rodrigues, Eric Durand, Marie-Stéphanie Aschtgen, Stéphanie Blangy, Miguel Ortiz-Lombardia, Badreddine Douzi, Christian Cambillau, Eric Cascales

Publikováno v: PLoS Pathogens, Vol 7, Iss 11, p e1002386 (2011)

Type VI secretion systems (T6SS) are trans-envelope machines dedicated to the secretion of virulence factors into eukaryotic or prokaryotic cells, therefore required for pathogenesis and/or for competition towards neighboring bacteria. The T6SS appar

Externí odkaz: https://doaj.org/article/85565310bbf5449eae0b500910e742f9

Polo kinase regulates the localization and activity of the chromosomal passenger complex in meiosis and mitosis in Drosophila melanogaster

Autor: Mar Carmena, Miguel Ortiz Lombardia, Hiromi Ogawa, William C. Earnshaw

Publikováno v: Open Biology, Vol 4, Iss 11 (2014)

Cell cycle progression is regulated by members of the cyclin-dependent kinase (CDK), Polo and Aurora families of protein kinases. The levels of expression and localization of the key regulatory kinases are themselves subject to very tight control. Th

Externí odkaz: https://doaj.org/article/cc3cda253de442b8b067f1983bdb3ecc

The 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding

Autor: Maria Chechik, Stefano Benini, Sigrun Polier, Mikhail B. Shevtsov, Miguel Ortiz Lombardia, Andrew P. Leech, Juan C. Alonso

Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69:376-381

DNA packaging in tailed bacteriophages and in evolutionarily related herpesviruses is controlled by a viral-encoded terminase. As in a number of other phages, in theBacillus subtilisbacteriophages SF6 and SPP1 the terminase complex consists of two pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39c30643566061d78248405a0696345b
https://doi.org/10.1107/s1744309113004399

Crystallization and preliminary crystallographic analysis of a novel cytochrome P450 from Mycobacterium tuberculosis

Autor: Graeme A Reid, Miguel Ortiz Lombardia, Stuart L. Rivers, Alison Richmond, Malcolm D. Walkinshaw, David Leys, Christopher G. Mowat, A. Stephen K. Chapman, Pedro M. Alzari, Kirsty J. McLean, Andrew W. Munro

Publikováno v: Mowat, C, Leys, D, McLean, K, Rivers, S, Richmond, A, Munro, A, Lombardia, M O, Alzari, P, Reid, G, Chapman, S & Walkinshaw, M 2002, ' Crystallization and preliminary crystallographic analysis of a novel cytochrome P450 from Mycobacterium tuberculosis ', Acta Crystallographica Section D: Biological Crystallography, vol. 58, pp. 704-705 . https://doi.org/10.1107/S0907444902002676
Acta Crystallographica Section D: Biological Crystallography
Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2002, 58 (4), pp.704-705. ⟨10.1107/s0907444902002676⟩
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2002, 58 (4), pp.704-705. ⟨10.1107/s0907444902002676⟩

International audience; The product of the Rv2276 gene of Mycobacterium tuberculosis is a cytochrome P450 (P450 MT2, CYP121) which has been shown to bind tightly to a range of azole-based antifungal drugs (e.g. miconazole, clotrimazole). These drugs

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7f2f0d8def359c76eda9fc26b872092
https://hdl.handle.net/20.500.11820/67ab0800-b091-4269-8f91-f2c1831b6056