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![[Figure 1]](jc5064fig1mag.jpg)
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Figure 1
Crystal structures and conformational changes accompanying ligand-bound LrGtfC100-23. (a, b) Details of the binding of UDP and the UDP-GlcNAc sugar donor (magenta C atoms), respectively, to LrGtfC100-23. The ligands and neighboring residues (labeled) are shown in stick format with a cartoon representation of the enzyme. Polar interactions are indicated by black dashed lines. A ligand omit map calculated contoured at 3σ is shown as a blue mesh in both panels. Note that here and in subsequent panels, residues 1–67 have been removed for clarity and so the hydrogen-bond interaction of the α-phosphate of ligands with the side chain of Thr16 is not seen. (c, d) Conformational changes observed during ligand binding. (c) A superposition of the N-terminal acceptor-binding domains of the apo (yellow cartoon, yellow C atoms) and sugar donor-bound (magenta cartoon, magenta C atoms) structures. Bound UDP-GlcNAc is shown in stick format with a molecular-surface rendering. Residues 103 and 112 (red text) delimit a flexible region of polypeptide adjacent to the binding site in the apo structure. (d) A superposition of the sugar donor-bound (orange cartoon, orange C atoms) and UDP-bound (gray cartoon, gray C atoms) enzyme structures. Bound UDP is shown in stick format. For each structure selected residues are shown in stick format and with a selection of hydrogen-bond interactions indicated by black dashed lines. |
![[Figure 1]](jc5064fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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