Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.
Regni, C., Shackelford, G.S., Beamer, L.J.(2006) Acta Crystallogr Sect F Struct Biol Cryst Commun 62: 722-726
- PubMed: 16880541 
- DOI: https://doi.org/10.1107/S1744309106025887
- Primary Citation of Related Structures:  
2H4L, 2H5A - PubMed Abstract: 
Two complexes of the enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa with a slow substrate and with an inhibitor have been characterized by X-ray crystallography. Both ligands induce an interdomain rearrangement in the enzyme that creates a highly buried active site. Comparisons with enzyme-substrate complexes show that the inhibitor xylose 1-phosphate utilizes many of the previously observed enzyme-ligand interactions. In contrast, analysis of the ribose 1-phosphate complex reveals a combination of new and conserved enzyme-ligand interactions for binding. The ability of PMM/PGM to accommodate these two pentose phosphosugars in its active site may be relevant for future efforts towards inhibitor design.
Organizational Affiliation: 
Department of Structural Biology, St Jude Children's Research Hospital, 332 North Lauderdale M/S 311, Memphis, TN 38105, USA.