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PDBsum entry 1viw

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protein ligands metals Protein-protein interface(s) links
Complex (glycosidase/inhibitor) PDB id
1viw
Jmol
Contents
Protein chains
471 a.a. *
198 a.a. *
Ligands
NAG-NAG ×2
Metals
_CA
_CL
* Residue conservation analysis
PDB id:
1viw
Name: Complex (glycosidase/inhibitor)
Title: Tenebrio molitor alpha-amylase-inhibitor complex
Structure: Alpha-amylase. Chain: a. Alpha-amylase-inhibitor. Chain: b. Synonym: alpha-ai
Source: Tenebrio molitor. Yellow mealworm. Organism_taxid: 7067. Other_details: larvae. Phaseolus vulgaris. Organism_taxid: 3885. Organ: seed
Biol. unit: Tetramer (from PQS)
Resolution:
3.00Å     R-factor:   0.230     R-free:   0.291
Authors: V.Nahoum,M.P.Egloff,F.Payan
Key ref:
V.Nahoum et al. (1999). A plant-seed inhibitor of two classes of alpha-amylases: X-ray analysis of Tenebrio molitor larvae alpha-amylase in complex with the bean Phaseolus vulgaris inhibitor. Acta Crystallogr D Biol Crystallogr, 55, 360-362. PubMed id: 10089450 DOI: 10.1107/S0907444998010701
Date:
21-Jul-98     Release date:   22-Jul-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P56634  (AMY_TENMO) -  Alpha-amylase
Seq:
Struc:
471 a.a.
471 a.a.*
Protein chain
Pfam   ArchSchema ?
P02873  (LEA1_PHAVU) -  Alpha-amylase inhibitor 1
Seq:
Struc:
246 a.a.
198 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: 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!
  Biological process     metabolic process   3 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
DOI no: 10.1107/S0907444998010701 Acta Crystallogr D Biol Crystallogr 55:360-362 (1999)
PubMed id: 10089450  
 
 
A plant-seed inhibitor of two classes of alpha-amylases: X-ray analysis of Tenebrio molitor larvae alpha-amylase in complex with the bean Phaseolus vulgaris inhibitor.
V.Nahoum, F.Farisei, V.Le-Berre-Anton, M.P.Egloff, P.Rougé, E.Poerio, F.Payan.
 
  ABSTRACT  
 
The alpha-amylase from Tenebrio molitor larvae (TMA) has been crystallized in complex with the alpha-amylase inhibitor (alpha-AI) from the bean Phaseolus vulgaris. A molecular-replacement solution of the structure was obtained using the refined pig pancreatic alpha-amylase (PPA) and alpha-AI atomic coordinates as starting models. The structural analysis showed that although TMA has the typical structure common to alpha-amylases, large deviations from the mammalian alpha-amylase models occur in the loops. Despite these differences in the interacting loops, the bean inhibitor is still able to inhibit both the insect and mammalian alpha-amylase.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 A stereoview of the superimposed C backbone traces of TMA (red) and PPA (blue) regions interacting with -AI (one monomer; green). The yellow and green spheres indicate the calcium and chloride ions present in the TMA structure, respectively.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 360-362) copyright 1999.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference Google scholar

  PubMed id Reference
18784084 M.E.Caines, H.Zhu, M.Vuckovic, L.M.Willis, S.G.Withers, W.W.Wakarchuk, and N.C.Strynadka (2008).
The Structural Basis for T-antigen Hydrolysis by Streptococcus pneumoniae: A TARGET FOR STRUCTURE-BASED VACCINE DESIGN.
  J Biol Chem, 283, 31279-31283.
PDB code: 3ecq
17444520 K.F.Lin, T.R.Lee, P.H.Tsai, M.P.Hsu, C.S.Chen, and P.C.Lyu (2007).
Structure-based protein engineering for alpha-amylase inhibitory activity of plant defensin.
  Proteins, 68, 530-540.
PDB code: 2gl1
16544327 Y.J.Liu, C.S.Cheng, S.M.Lai, M.P.Hsu, C.S.Chen, and P.C.Lyu (2006).
Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids.
  Proteins, 63, 777-786.
PDB code: 1ti5
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.  
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
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.