2h4l
From Proteopedia
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Complex of PMM/PGM with ribose 1-phosphate
Overview
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.
About this Structure
2H4L is a Single protein structure of sequence from Pseudomonas aeruginosa with R1P and ZN as ligands. Full crystallographic information is available from OCA.
Reference
Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor., Regni C, Shackelford GS, Beamer LJ, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):722-6. Epub 2006 Jul 24. PMID:16880541
Page seeded by OCA on Wed Nov 21 11:32:33 2007
