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

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Type‐II NADH:quinone oxidoreductase from Staphylococcus aureus has two distinct binding sites and is rate limited by quinone reduction

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MOLECULAR MICROBIOLOGY, Vol. 98, Iss. 2, 2015-10 ,pp. : 272-288

John Wiley & Sons Inc

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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

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

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Crosslinking of peptidoglycan by l,d‐transpeptidases allows bacteria to bypass the antibacterial activity of many betalactams as well as vancomycin. NMR studies of the Enterococcus faeciuml,d‐transpeptidase have identified the binding sites for the acyl donor and the acyl acceptor of the peptidoglycan cross‐linking reaction. For details, see the article by Triboulet et al. on pp. 90–100 of this issue.

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MOLECULAR MICROBIOLOGY, Vol. 950-382X, Iss. 1, 2015-10 ,pp. : i-i

John Wiley & Sons Inc

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Crosslinking of peptidoglycan by l,d‐transpeptidases allows bacteria to bypass the antibacterial activity of many betalactams as well as vancomycin. NMR studies of the Enterococcus faeciuml,d‐transpeptidase have identified the binding sites for the acyl donor and the acyl acceptor of the peptidoglycan cross‐linking reaction. For details, see the article by Triboulet et al. on pp. 90–100 of this issue.

By  

MOLECULAR MICROBIOLOGY, Vol. 98, Iss. 1, 2015-10 ,pp. : i-i

John Wiley & Sons Inc

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