Structure of Bacillus anthracis AtxA, a dimeric virulence regulator, with one subunit color‐coded and one in gray. AtxA contains two phosphoenolpyruvate:carbohydrate phosphotransferase system‐related domains (PRD1 and PRD2; blue and green) and two helix‐turn‐helix (HTH) containing DNA‐binding domains (red and purple). Two histidines that are phosphorylated are highlighted in one of the subunits of the dimer. For details, see the article by Hammerstrom et al. on pp. 426–441 of this issue

Publisher： John Wiley & Sons Inc

E-ISSN： 1365-2958|95|3|i-i

ISSN： 0950-382x

Source： MOLECULAR MICROBIOLOGY, Vol.95, Iss.3, 2015-02, pp. : i-i

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AtxA multimerization, phosphorylation and activity

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MOLECULAR MICROBIOLOGY, Vol. 95, Iss. 3, 2015-02 ,pp. : 426-441

John Wiley & Sons Inc

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Fluorescence images of yeast cells showing mitochondria in red and two subunits of a presumed trimeric complex in green (left images: Rho5‐GFP, right images: Dck1‐GFP). Plasma membrane localization of the latter observed under standard growth conditions (upper row) is rapidly switched to mitochondria after application of oxidative stress. For details, see the article by Schmitz et al. on pp. 306–324 of this issue.

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MOLECULAR MICROBIOLOGY, Vol. 96, Iss. 2, 2015-04 ,pp. : i-i

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The type‐II NADH:quinone oxidoreductase (NDH‐2) from Staphylococcus aureus has been recognized as a potential target for antimicrobial therapy. Structural and biochemical studies reveal that NDH‐2 is a dimeric protein with distinct binding sites for the two substrates (NADH and quinones). Kinetic studies identify quinone reduction as the rate limiting step. For details, see the article by Sena et al. on pp. 272–288 of this issue.

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MOLECULAR MICROBIOLOGY, Vol. 950-382X, Iss. 2, 2015-10 ,pp. : i-i

John Wiley & Sons Inc

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The type‐II NADH:quinone oxidoreductase (NDH‐2) from Staphylococcus aureus has been recognized as a potential target for antimicrobial therapy. Structural and biochemical studies reveal that NDH‐2 is a dimeric protein with distinct binding sites for the two substrates (NADH and quinones). Kinetic studies identify quinone reduction as the rate limiting step. For details, see the article by Sena et al. on pp. 272–288 of this issue.

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MOLECULAR MICROBIOLOGY, Vol. 98, Iss. 2, 2015-10 ,pp. : i-i

John Wiley & Sons Inc

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Side and top views of electron microscopy‐based 3D reconstructions of Escherichia coli NorR in complex with DNA showing DNA (purple) stabilising the NorR hexamer through interacting with multiple domains. See the related article, “The structural basis for enhancerdependent assembly and activation of the AAA transcriptional activator” by Bush et al. in Vol. 95, issue 1 (pp. 17–30)

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MOLECULAR MICROBIOLOGY, Vol. 95, Iss. 4, 2015-02 ,pp. : i-i

John Wiley & Sons Inc

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