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Thalis Project 2011 (EVOTRANS)

EVOTRANS Figure 1

N-ethymaleimide (NEM)-sensitive positions of the important set of residues found in permease XanQ. Such residues (circles with red outlines) may not be at the binding site per se but at the periphery; in the latter case, the maleimidyl adduct allows binding but blocks translocation of substrate by blocking the conformational switch in the alternating access mechanism [see: Georgopoulou et al., J Biol Chem 285, 19422-33 (2010)]

EVOTRANS Figure 2

Structure-topology model of the proline transporter PrnB (APC superfamily) threaded on the x-ray structures of LeuT (NSS family) and Mhp1 (NCS1 family). Putatively important residues are indicated with asterisks. [after Vangelatos et al., Mol Membr Biol 26, 356-70 (2009)]

EVOTRANS Figure 3

Initial molecular docking of guanine (G tautomer, pH 7.0) at the binding site of the fungal nucleobase transporter FcyB. Residues involved in binding are indicated [for the functional identification of FcyB see: Vlanti and Diallinas, Mol Microbiol 68, 959-77 (2008)]

EVOTRANS Figure 4

The general rocker-switch (N6-C6) motif of MFS superfamily (A) and conserved sequence motifs of the nitrate/nitrite porter (NNP) family of MFS superfamily (B). The non-MFS permease MelB can be threaded on the x-ray structure of the MFS-prototype LacY, as shown in A [after Yousef and Guan, PNAS 106, 15291-6 (2009)] ; the new putative nitrate transporters from biodegrading soil bacteria conserve characteristic motifs of the NNP family, including binding-site Gly residues (TM5), a presumed nitrate binding-site Arg (TM8) and the nitrate-signature motif (TM11), as shown in B [see: Unkles et al., PNAS 101, 17549-54 (2004)]