Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 62(Pt 8): 722-6, 2006 Aug 01.
Article
en En
| MEDLINE
| ID: mdl-16880541
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fosfoglucomutasa
/
Pseudomonas aeruginosa
/
Fosfotransferasas (Fosfomutasas)
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2006
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Reino Unido