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PDBsum entry 2h4l
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References listed in PDB file
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Key reference
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Title
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Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.
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Authors
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C.Regni,
G.S.Shackelford,
L.J.Beamer.
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Ref.
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Acta Crystallograph Sect F Struct Biol Cryst Commun, 2006,
62,
722-726.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 2.
Figure 2 PMM/PGM in complex with X1P and R1P. The protein is
colored by domain, with blue, light blue, pink and magenta for
domains 1, 2, 3 and 4, respectively. (a) Ribbon diagram of
PMM/PGM with X1P (yellow) and R1P (green) bound in the active
site. (b) Superposition of the C^  atoms
of the R1P complex with those of apo-PMM/PGM (PDB code 1k2y )
shown in gray, demonstrating the rotation of domain 4. Close-up
view of the active site of PMM/PGM with bound (c) X1P and (d)
R1P. For clarity, only interactions between side chains of the
enzyme and ligands are highlighted; water molecules are shown as
spheres. (e) For comparison, a superposition of the slow
substrate R1P and a preferred substrate G1P (cyan) in the active
site of PMM/PGM is shown.
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallograph Sect F Struct Biol Cryst Commun
(2006,
62,
722-726)
copyright 2006.
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