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Figure 4
A model for substrate binding in the active site. LpxC is depicted as a van der Waals surface. The experimental models of UDP and TU-514, derived from crystal structures, provide the template to model the substrate. The ligands are shown as sticks. The experimentally derived C atoms are coloured black and the modelled substrate C atoms cyan. Conserved residues in the LpxC active site (at a level of >60%) are coloured by type: histidines green, lysine blue, aspartate red, threonine slate-blue, aromatic phenylalanines salmon, glycine and leucine magenta. The catalytic Zn2+ and a water molecule implicated in the mechanism are shown as grey and marine spheres, respectively, and ligand atoms are depicted as in Figs. 2[link] and 3[link].

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 62| Part 11| October 2006| Pages 1082-1086
doi:10.1107/S1744309106041893
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