1dhk: Difference between revisions
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[[Image:1dhk.gif|left|200px]] | [[Image:1dhk.gif|left|200px]] | ||
'''STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE''' | {{Structure | ||
|PDB= 1dhk |SIZE=350|CAPTION= <scene name='initialview01'>1dhk</scene>, resolution 1.85Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DHK is a [ | 1DHK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHK OCA]. | ||
==Reference== | ==Reference== | ||
Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex., Bompard-Gilles C, Rousseau P, Rouge P, Payan F, Structure. 1996 Dec 15;4(12):1441-52. PMID:[http:// | Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex., Bompard-Gilles C, Rousseau P, Rouge P, Payan F, Structure. 1996 Dec 15;4(12):1441-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8994970 8994970] | ||
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Phaseolus vulgaris]] | [[Category: Phaseolus vulgaris]] | ||
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[[Category: porcine]] | [[Category: porcine]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:38:34 2008'' | ||
Revision as of 11:38, 20 March 2008
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| , resolution 1.85Å | |||||||
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| Ligands: | , and | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE
OverviewOverview
BACKGROUND: alpha-Amylases catalyze the hydrolysis of glycosidic linkages in starch and other related polysaccharides. The alpha-amylase inhibitor (alpha-Al) from the bean Phaseolus vulgaris belongs to a family of plant defence proteins and is a potent inhibitor of mammalian alpha-amylases. The structure of pig pancreatic alpha-amylase (PPA) in complex with both a carbohydrate inhibitor (acarbose) and a proteinaceous inhibitor (Tendamistat) is known, but the catalytic mechanism is poorly understood. RESULTS: The crystal structure of pig pancreatic alpha-amylase complexed with alpha-Al was refined to 1.85 A resolution. It reveals that in complex with PPA, the inhibitor has the typical dimer structure common to legume lectins. Two hairpin loops extending out from the jellyroll fold of a monomer interact directly with the active site region of the enzyme molecule, with the inhibitor molecule filling the whole substrate-docking region of the PPA. The inhibitor makes substrate-mimetic interactions with binding subsites of the enzyme and targets catalytic residues in the active site. Binding of inhibitor induces structural changes at the active site of the enzyme. CONCLUSIONS: The present analysis reveals that there are extensive interactions between the inhibitor and residues that are highly conserved in the active site of alpha-amylases; alpha-Al1 inactivates PPA through elaborate blockage of substrate-binding sites. It provides a basis to design peptide analogue inhibitors. alpha-Amylase inhibition is of interest from several points of view, for example the treatment of diabetes and for crop protection.
About this StructureAbout this Structure
1DHK is a Protein complex structure of sequences from Phaseolus vulgaris and Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex., Bompard-Gilles C, Rousseau P, Rouge P, Payan F, Structure. 1996 Dec 15;4(12):1441-52. PMID:8994970
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