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PDBsum entry 1hss
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protein Protein-protein interface(s) links
Cereal inhibitor PDB id
1hss

 

 

 

 

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Contents
Protein chains
111 a.a. *
Waters ×264
* Residue conservation analysis
PDB id:
1hss
Name: Cereal inhibitor
Title: 0.19 alpha-amylase inhibitor from wheat
Structure: 0.19 alpha-amylase inhibitor. Chain: a, b, c, d
Source: Triticum aestivum. Bread wheat. Organism_taxid: 4565. Organ: kernel
Biol. unit: Dimer (from PDB file)
Resolution:
2.06Å     R-factor:   0.187     R-free:   0.223
Authors: Y.Oda,K.Fukuyama
Key ref:
Y.Oda et al. (1997). Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 A resolution. Biochemistry, 36, 13503-13511. PubMed id: 9354618 DOI: 10.1021/bi971307m
Date:
01-Jul-97     Release date:   01-Jul-98    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P01085  (IAA1_WHEAT) -  Alpha-amylase inhibitor 0.19 from Triticum aestivum
Seq:
Struc: 		124 a.a.
111 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1021/bi971307m Biochemistry 36:13503-13511 (1997)
PubMed id: 9354618  
 
 
Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 A resolution.
Y.Oda, T.Matsunaga, K.Fukuyama, T.Miyazaki, T.Morimoto.
 
  ABSTRACT  
 
The crystal structure of 0.19 alpha-amylase inhibitor (0.19 AI) from wheat kernel was determined by the multiple-isomorphous replacement method coupled with density modification and noncrystallographic symmetry averaging and then refined by simulated annealing using diffraction data to 2.06 A resolution (R = 18.7%, free R = 22.3%). The asymmetric unit has four molecules of 0.19 AI, each comprised of 124 amino acid residues. Electron density for residues 1-4 and 69-77 is absent in all subunits, probably because of the intrinsic flexibility of these segments. Each subunit has four major alpha-helices and one one-turn helix which are arranged in the up-and-down manner, maintaining the favorable packing modes of the alpha-helices. 0.19 AI, however, has two short antiparallel beta-strands. All 10 cysteine residues in 0.19 AI form disulfide bonds (C6-C52, C20-C41, C28-C83, C42-C99, and C54-C115), consistent with the assignments made biochemically for 0.28 AI from wheat kernel and by NMR analysis of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds (RBI). The disulfide bond patterns in these AIs are similar to those in the hydrophobic protein from soybean (HPS), which lack only the bond corresponding to C28-C83 in 0.19 AI. Extensive interactions occurred between particular pairs of 0.19 AI subunits, mainly involving hydrophobic residues. Comparisons of the structures of 0.19 AI, RBI, and HPS showed that the arrangements of the major alpha-helices are similar but the conformations of the remaining residues differ markedly. The present X-ray analysis for 0.19 AI and the NMR analysis for RBI suggest that all the AIs in this family have a common fold. The alpha-amylase binding site is discussed on the basis of the tertiary and quaternary structures of 0.19 AI together with biochemical and spectroscopic data for AIs.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18366725 J.R.Wang, Y.M.Wei, X.Y.Long, Z.H.Yan, E.Nevo, B.R.Baum, and Y.L.Zheng (2008).
Molecular evolution of dimeric alpha-amylase inhibitor genes in wild emmer wheat and its ecological association.
  BMC Evol Biol, 8, 91.  
18060568 J.R.Wang, Y.M.Wei, Z.H.Yan, and Y.L.Zheng (2008).
SNP and haplotype identification of the wheat monomeric alpha-amylase inhibitor genes.
  Genetica, 134, 277-285.  
16177913 K.Liu, H.Jiang, S.L.Moore, C.B.Watkins, and M.M.Jahn (2006).
Isolation and characterization of a lipid transfer protein expressed in ripening fruit of Capsicum chinense.
  Planta, 223, 672-683.  
16279937 J.T.Christeller (2005).
Evolutionary mechanisms acting on proteinase inhibitor variability.
  FEBS J, 272, 5710-5722.  
12493826 R.Cazalis, T.Aussenac, L.Rhazi, A.Marin, and J.F.Gibrat (2003).
Homology modeling and molecular dynamics simulations of the N-terminal domain of wheat high molecular weight glutenin subunit 10.
  Protein Sci, 12, 34-43.  
12472696 E.van der Graaff, P.J.Hooykaas, and B.Keller (2002).
Activation tagging of the two closely linked genes LEP and VAS independently affects vascular cell number.
  Plant J, 32, 819-830.  
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.  
11294620 J.Qi, J.Wu, G.A.Somkuti, and J.T.Watson (2001).
Determination of the disulfide structure of sillucin, a highly knotted, cysteine-rich peptide, by cyanylation/cleavage mass mapping.
  Biochemistry, 40, 4531-4538.  
11137459 J.Iulek, O.L.Franco, M.Silva, C.T.Slivinski, C.Bloch, D.J.Rigden, and M.F.Grossi de Sá (2000).
Purification, biochemical characterisation and partial primary structure of a new alpha-amylase inhibitor from Secale cereale (rye).
  Int J Biochem Cell Biol, 32, 1195-1204.  
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.  
10713993 M.J.Pandya, R.B.Sessions, P.B.Williams, C.E.Dempsey, A.S.Tatham, P.R.Shewry, and A.R.Clarke (2000).
Structural characterization of a methionine-rich, emulsifying protein from sunflower seed.
  Proteins, 38, 341-349.  
10759839 O.L.Franco, D.J.Rigden, F.R.Melo, C.Bloch, C.P.Silva, and M.F.Grossi de Sá (2000).
Activity of wheat alpha-amylase inhibitors towards bruchid alpha-amylases and structural explanation of observed specificities.
  Eur J Biochem, 267, 2166-2173.  
10508777 P.J.Pereira, V.Lozanov, A.Patthy, R.Huber, W.Bode, S.Pongor, and S.Strobl (1999).
Specific inhibition of insect alpha-amylases: yellow meal worm alpha-amylase in complex with the amaranth alpha-amylase inhibitor at 2.0 A resolution.
  Structure, 7, 1079-1088.
PDB code: 1clv
10089391 S.Gourinath, A.Srinivasan, and T.P.Singh (1999).
Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.9 A resolution.
  Acta Crystallogr D Biol Crystallogr, 55, 25-30.
PDB code: 1jfo
9873419 A.D.Abell, M.J.Ratcliffe, and J.Gerrard (1998).
Ascorbic acid-based inhibitors of alpha-amylases.
  Bioorg Med Chem Lett, 8, 1703-1706.  
9799488 C.A.Behnke, V.C.Yee, I.L.Trong, L.C.Pedersen, R.E.Stenkamp, S.S.Kim, G.R.Reeck, and D.C.Teller (1998).
Structural determinants of the bifunctional corn Hageman factor inhibitor: x-ray crystal structure at 1.95 A resolution.
  Biochemistry, 37, 15277-15288.
PDB codes: 1bea 1bfa
9687373 S.Strobl, K.Maskos, G.Wiegand, R.Huber, F.X.Gomis-Rüth, and R.Glockshuber (1998).
A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution.
  Structure, 6, 911-921.
PDB code: 1tmq
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 code is shown on the right.

 

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