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PDBsum entry 1jfh
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References listed in PDB file
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Key reference
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Title
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Structure of a pancreatic alpha-Amylase bound to a substrate analogue at 2.03 a resolution.
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Authors
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M.Qian,
S.Spinelli,
H.Driguez,
F.Payan.
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Ref.
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Protein Sci, 1997,
6,
2285-2296.
[DOI no: ]
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PubMed id
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Abstract
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The structure of pig pancreatic alpha-amylase in complex with carbohydrate
inhibitor and proteinaceous inhibitors is known but the successive events
occurring at the catalytic center still remain to be elucidated. The X-ray
structure analysis of a crystal of pig pancreatic alpha-amylase (PPA, EC
3.2.1.1.) soaked with an enzyme-resistant substrate analogue, methyl
4,4'-dithio-alpha-maltotrioside, showed electron density corresponding to the
binding of substrate analogue molecules at the active site and at the "second
binding site." The electron density observed at the active site was interpreted
in terms of overlapping networks of oligosaccharides, which show binding of
substrate analogue molecules at subsites prior to and subsequent to the cleavage
site. A weaker patch of density observed at subsite -1 (using a nomenclature
where the site of hydrolysis is taken to be between subsites -1 and +1) was
modeled with water molecules. Conformational changes take place upon substrate
analogue binding and the "flexible loop" that constitutes the surface edge of
the active site is observed in a specific conformation. This confirms that this
loop plays an important role in the recognition and binding of the ligand. The
crystal structure was refined at 2.03 A resolution, to an R-factor of 16.0
(Rfree, 18.5).
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Secondary reference #1
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Title
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Crystal structure of pig pancreatic alpha-Amylase isoenzyme ii, In complex with the carbohydrate inhibitor acarbose.
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Authors
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C.Gilles,
J.P.Astier,
G.Marchis-Mouren,
C.Cambillau,
F.Payan.
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Ref.
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Eur J Biochem, 1996,
238,
561-569.
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PubMed id
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Secondary reference #2
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Title
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Carbohydrate binding sites in a pancreatic alpha-Amylase-Substrate complex, Derived from x-Ray structure analysis at 2.1 a resolution.
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Authors
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M.Qian,
R.Haser,
F.Payan.
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Ref.
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Protein Sci, 1995,
4,
747-755.
[DOI no: ]
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PubMed id
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Figure 5.
Fig. 5. Stackingfeature between theplane of te
tryptophan ring f residue 388 andthehydropho-
bicregionofthemaltoseunitboundatthe ``sec-
ondsite'' of theenzyme molecule. Dottedsurface
representsthevanderWaalsradiioftheatoms.
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Figure 7.
Fig. 7. Detailed stereo view of the arrangement of
protein sidechainsinvolved in with the
monosaccharide. Calcium ion is in
with the sugar unit through its water ligand.
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The above figures are
reproduced from the cited reference
which is an Open Access publication published by the Protein Society
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Secondary reference #3
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Title
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The active center of a mammalian alpha-Amylase. Structure of the complex of a pancreatic alpha-Amylase with a carbohydrate inhibitor refined to 2.2-A resolution.
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Authors
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M.Qian,
R.Haser,
G.Buisson,
E.Duée,
F.Payan.
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Ref.
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Biochemistry, 1994,
33,
6284-6294.
[DOI no: ]
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PubMed id
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Secondary reference #4
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Title
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Structure and molecular model refinement of pig pancreatic alpha-Amylase at 2.1 a resolution.
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Authors
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M.Qian,
R.Haser,
F.Payan.
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Ref.
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J Mol Biol, 1993,
231,
785-799.
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PubMed id
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