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PDBsum entry 1ose

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protein ligands metals links
Hydrolase PDB id
1ose
Jmol
Contents
Protein chain
496 a.a. *
Ligands
AC1-GLC-AC1-BGC
BGC
Metals
_CA
_CL
Waters ×403
* Residue conservation analysis
PDB id:
1ose
Name: Hydrolase
Title: Porcine pancreatic alpha-amylase complexed with acarbose
Structure: Porcine alpha-amylase. Chain: a. Synonym: ppa. Ec: 3.2.1.1
Source: Sus scrofa. Pig. Organism_taxid: 9823. Organ: pancreas
Resolution:
2.30Å     R-factor:   0.176     R-free:   0.222
Authors: C.Gilles,F.Payan
Key ref: C.Gilles et al. (1996). Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose. Eur J Biochem, 238, 561-569. PubMed id: 8681972
Date:
20-Mar-96     Release date:   01-Apr-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00690  (AMYP_PIG) -  Pancreatic alpha-amylase
Seq:
Struc:
511 a.a.
496 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.1  - Alpha-amylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides and polysaccharides.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     metabolic process   3 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
Eur J Biochem 238:561-569 (1996)
PubMed id: 8681972  
 
 
Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose.
C.Gilles, J.P.Astier, G.Marchis-Mouren, C.Cambillau, F.Payan.
 
  ABSTRACT  
 
Two different crystal forms of pig pancreatic alpha-amylase isoenzyme II (PPAII), free and complexed to a carbohydrate inhibitor (acarbose), have been compared together and to previously reported structures of PPAI. A crystal form obtained at 4 degrees C, containing nearly 72% solvent, made it possible to obtain a new complex with acarbose, different from a previous one obtained at 20 degrees C [Qian, M., Buisson, G., Duée, E., Haser, H. & Payan, F. (1994) Biochemistry 33, 6284-6294]. In the present form, six contiguous subsites of the enzyme active site are occupied by the carbohydrate ligand; the structural data indicate that the binding site is capable of holding more than the five glucose units of the scheme proposed through kinetic studies. A monosaccharide ring bridging two protein molecules related by the crystal packing is located on the surface, at a distance of 2.0 nm from the reducing end of the inhibitor ligand; the symmetry-related glucose ring in the crystal lattice is found 1.5 nm away from the non-reducing end of the inhibitor ligand.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20222716 S.B.Larson, J.S.Day, and A.McPherson (2010).
X-ray crystallographic analyses of pig pancreatic alpha-amylase with limit dextrin, oligosaccharide, and alpha-cyclodextrin.
  Biochemistry, 49, 3101-3115.
PDB codes: 3l2l 3l2m
18951906 C.Ragunath, S.G.Manuel, V.Venkataraman, H.B.Sait, C.Kasinathan, and N.Ramasubbu (2008).
Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding.
  J Mol Biol, 384, 1232-1248.  
18505459 Y.T.Pan, J.D.Carroll, N.Asano, I.Pastuszak, V.K.Edavana, and A.D.Elbein (2008).
Trehalose synthase converts glycogen to trehalose.
  FEBS J, 275, 3408-3420.  
17044042 C.Albenne, L.K.Skov, V.Tran, M.Gajhede, P.Monsan, M.Remaud-Siméon, and G.André-Leroux (2007).
Towards the molecular understanding of glycogen elongation by amylosucrase.
  Proteins, 66, 118-126.  
15969461 J.Hubert, L.Dolecková-Maresová, J.Hýblová, I.Kudlíková, V.Stejskal, and M.Mares (2005).
In vitro and in vivo inhibition of alpha-amylases of stored-product mite Acarus siro.
  Exp Appl Acarol, 35, 281-291.  
15356864 G.André, and V.Tran (2004).
Putative implication of alpha-amylase loop 7 in the mechanism of substrate binding and reaction products release.
  Biopolymers, 75, 95.  
15043869 H.K.Kang, J.H.Lee, D.Kim, D.F.Day, J.F.Robyt, K.H.Park, and T.W.Moon (2004).
Cloning and expression of Lipomyces starkeyi alpha-amylase in Escherichia coli and determination of some of its properties.
  FEMS Microbiol Lett, 233, 53-64.  
12482867 A.Linden, O.Mayans, W.Meyer-Klaucke, G.Antranikian, and M.Wilmanns (2003).
Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc.
  J Biol Chem, 278, 9875-9884.
PDB codes: 1mwo 1mxd 1mxg
14617662 M.Kagawa, Z.Fujimoto, M.Momma, K.Takase, and H.Mizuno (2003).
Crystal structure of Bacillus subtilis alpha-amylase in complex with acarbose.
  J Bacteriol, 185, 6981-6984.
PDB code: 1ua7
12392547 G.Gyémánt, G.Hovánszki, and L.Kandra (2002).
Subsite mapping of the binding region of alpha-amylases with a computer program.
  Eur J Biochem, 269, 5157-5162.  
11856298 O.L.Franco, D.J.Rigden, F.R.Melo, and M.F.Grossi-De-Sá (2002).
Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases.
  Eur J Biochem, 269, 397-412.  
11443082 M.Hemker, A.Stratmann, K.Goeke, W.Schröder, J.Lenz, W.Piepersberg, and H.Pape (2001).
Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. strain SE50.
  J Bacteriol, 183, 4484-4492.  
11168426 R.Koukiekolo, V.Desseaux, Y.Moreau, G.Marchis-Mouren, and M.Santimone (2001).
Mechanism of porcine pancreatic alpha-amylase. Inhibition of amylose and maltopentaose hydrolysis by alpha-, beta- and gamma-cyclodextrins.
  Eur J Biochem, 268, 841-848.  
10769135 G.D.Brayer, G.Sidhu, R.Maurus, E.H.Rydberg, C.Braun, Y.Wang, N.T.Nguyen, C.M.Overall, and S.G.Withers (2000).
Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques.
  Biochemistry, 39, 4778-4791.
PDB codes: 1cpu 2cpu 3cpu
  11082203 I.Przylas, Y.Terada, K.Fujii, T.Takaha, W.Saenger, and N.Sträter (2000).
X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus. Implications for the synthesis of large cyclic glucans.
  Eur J Biochem, 267, 6903-6913.
PDB code: 1esw
11025543 J.Lehtiö, T.T.Teeri, and P.A.Nygren (2000).
Alpha-amylase inhibitors selected from a combinatorial library of a cellulose binding domain scaffold.
  Proteins, 41, 316-322.  
11128586 L.Kandra, and G.Gyémánt (2000).
Examination of the active sites of human salivary alpha-amylase (HSA).
  Carbohydr Res, 329, 579-585.  
10841756 T.J.Kim, C.S.Park, H.Y.Cho, S.S.Cha, J.S.Kim, S.B.Lee, T.W.Moon, J.W.Kim, B.H.Oh, and K.H.Park (2000).
Role of the glutamate 332 residue in the transglycosylation activity of ThermusMaltogenic amylase.
  Biochemistry, 39, 6773-6780.  
10872458 H.D.Ly, and S.G.Withers (1999).
Mutagenesis of glycosidases.
  Annu Rev Biochem, 68, 487-522.  
10491128 J.E.Nielsen, L.Beier, D.Otzen, T.V.Borchert, H.B.Frantzen, K.V.Andersen, and A.Svendsen (1999).
Electrostatics in the active site of an alpha-amylase.
  Eur J Biochem, 264, 816-824.  
10220320 M.O'Reilly, K.A.Watson, and L.N.Johnson (1999).
The crystal structure of the Escherichia coli maltodextrin phosphorylase-acarbose complex.
  Biochemistry, 38, 5337-5345.
PDB code: 2ecp
10491154 R.Koukiekolo, V.Le Berre-Anton, V.Desseaux, Y.Moreau, P.Rougé, G.Marchis-Mouren, and M.Santimone (1999).
Mechanism of porcine pancreatic alpha-amylase inhibition of amylose and maltopentaose hydrolysis by kidney bean (Phaseolus vulgaris) inhibitor and comparison with that by acarbose.
  Eur J Biochem, 265, 20-26.  
10082956 S.Darnis, N.Juge, X.J.Guo, G.Marchis-Mouren, A.Puigserver, and J.C.Chaix (1999).
Molecular cloning and primary structure analysis of porcine pancreatic alpha-amylase.
  Biochim Biophys Acta, 1430, 281-289.  
10387084 Z.Dauter, M.Dauter, A.M.Brzozowski, S.Christensen, T.V.Borchert, L.Beier, K.S.Wilson, and G.J.Davies (1999).
X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution.
  Biochemistry, 38, 8385-8392.
PDB codes: 1qho 1qhp
9649422 M.Lauwereys, M.Arbabi Ghahroudi, A.Desmyter, J.Kinne, W.Hölzer, E.De Genst, L.Wyns, and S.Muyldermans (1998).
Potent enzyme inhibitors derived from dromedary heavy-chain antibodies.
  EMBO J, 17, 3512-3520.  
9283074 A.M.Brzozowski, and G.J.Davies (1997).
Structure of the Aspergillus oryzae alpha-amylase complexed with the inhibitor acarbose at 2.0 A resolution.
  Biochemistry, 36, 10837-10845.
PDB code: 7taa
9345621 B.Henrissat, and G.Davies (1997).
Structural and sequence-based classification of glycoside hydrolases.
  Curr Opin Struct Biol, 7, 637-644.  
  9385631 M.Qian, S.Spinelli, H.Driguez, and F.Payan (1997).
Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03 A resolution.
  Protein Sci, 6, 2285-2296.
PDB code: 1jfh
8994970 C.Bompard-Gilles, P.Rousseau, P.Rougé, and F.Payan (1996).
Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex.
  Structure, 4, 1441-1452.
PDB code: 1dhk
8944767 M.Alkazaz, V.Desseaux, G.Marchis-Mouren, F.Payan, E.Forest, and M.Santimone (1996).
The mechanism of porcine pancreatic alpha-amylase. Kinetic evidence for two additional carbohydrate-binding sites.
  Eur J Biochem, 241, 787-796.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.