Fig. 4: R699 dimer creates a continuous cleft that may be involved in collagen binding. | Nature Communications

Fig. 4: R699 dimer creates a continuous cleft that may be involved in collagen binding.

From: Structural basis of collagen glucosyltransferase function and its serendipitous role in kojibiose synthesis

Fig. 4

a Surface representation of the R699 homodimer. The dimerization interface creates a continuous cleft flanked by the active sites. One of 2 Mn²⁺ atoms (slate) is shown within an active domain (cyan), and both N193 (white) residues are highlighted within the cleft. b, c Enzymatic activity assay of R699 using galactosylhydroxylysine (Gal-Hyl in b) or denatured bovine type I collagen (PureCol in c) as a substrate. Enzymatic activity was measured by detecting UDP production with a luciferase assay. Results are expressed as mean values (± S.D.) from triplicate biological samples (n = 3). For both panels, p values were determined using two-tailed Student’s t-tests.

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