Mutational studies of the xanthine permease XanQ of Escherichia coli, a paradigm for the nucleobase‐cation symporter‐2 (NCS2) family of transporters, identified a critical role for six Gly residues in the gate domain (orange ribbons) and a hydrogen bonding network (inset) involving Gln‐75 (TM2), Asp‐304 (TM9), Thr‐321 (β10) and Gln‐90 (β3) in the core domain. For details, see the article by Karena et al. on pp. 502–517 of this issue.

Publisher： John Wiley & Sons Inc

E-ISSN： 1365-2958|98|3|i-i

ISSN： 0950-382x

Source： MOLECULAR MICROBIOLOGY, Vol.98, Iss.3, 2015-10, pp. : i-i

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Analysis of conserved NCS2 motifs in the Escherichia coli xanthine permease XanQ

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MOLECULAR MICROBIOLOGY, Vol. 98, Iss. 3, 2015-10 ,pp. : 502-517

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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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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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