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Figure 1
(a) The crystal structure of the L. salivarius Tkt protomer has a V-shaped conformation that can be divided into three discrete domains. Secondary-structure elements are coloured yellow for β-strands and red for α-helices, with loop regions in grey. The TPP ligand molecule is shown in spherical representation and is coloured green. (b) Two Tkt protomers coloured red and blue associate through an extensive interface to form a functional dimer. Molecular-graphics figures were prepared using PyMOL (v.1.3r1; Schrödinger). (c) SEC-MALLS analysis of LsTkt. The continuous black line shows the normalized protein absorbance (arbitrary units) as a function of elution volume for the apoprotein and the dashed black line is that for LsTktA in the presence of 0.5 mM TPP. The red and blue scatter plots represent the molar-mass distributions of the presumed dimeric and monomeric species of the apoprotein and cofactor-bound protein, respectively.

ISSN: 2053-230X
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