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PDBsum entry 1smf
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Hydrolase/hydrolase inhibitor PDB id
1smf

 

 

 

 

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Contents
Protein chain
223 a.a. *
Ligands
CYS-THR-LYS-SER-
ILE-PRO-PRO-GLU-
CYS
Metals
_CA
Waters ×249
* Residue conservation analysis
PDB id:
1smf
Name: Hydrolase/hydrolase inhibitor
Title: Studies on an artificial trypsin inhibitor peptide derived from the mung bean inhibitor
Structure: Trypsin. Chain: e. Engineered: yes. Bowman-birk type trypsin inhibitor. Chain: i. Engineered: yes
Source: Bos taurus. Bovine. Organism_taxid: 9913. Tissue: pancreas.
Biol. unit: Dimer (from PQS)
Resolution:
2.10Å     R-factor:   0.190    
Authors: Q.Huang,Y.Li,S.Zhang,S.Liu,Y.Tang,C.Qi
Key ref: Y.Li et al. (1994). Studies on an artificial trypsin inhibitor peptide derived from the mung bean trypsin inhibitor: chemical synthesis, refolding, and crystallographic analysis of its complex with trypsin. J Biochem (tokyo), 116, 18-25. PubMed id: 7798176
Date:
24-Oct-92     Release date:   31-Jul-94    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00760  (TRY1_BOVIN) -  Serine protease 1 from Bos taurus
Seq:
Struc: 		246 a.a.
223 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.4  - trypsin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

 

 
J Biochem (tokyo) 116:18-25 (1994)
PubMed id: 7798176  
 
 
Studies on an artificial trypsin inhibitor peptide derived from the mung bean trypsin inhibitor: chemical synthesis, refolding, and crystallographic analysis of its complex with trypsin.
Y.Li, Q.Huang, S.Zhang, S.Liu, C.Chi, Y.Tang.
 
  ABSTRACT  
 
The active fragment with Lys at the reactive site of mung bean trypsin inhibitor (MBILF) is composed of two peptide chains, A1 of 26 residues and A2 of 9 residues linked via two disulfide bonds. In the present study, a peptide of 22 residue comprising the sequence of chain A1 from position 3 to 24 was synthesized by the solid-phase method. This synthetic peptide with six Cys residues contains a reactive site at position Lys11I-Ser12I (I denotes an inhibitor residue). Air oxidation and HPLC purification resulted in two antitrypsin active components, SPC1 and SPC2. Neither SPC1 nor SPC2 can stoichiometrically inhibit trypsin. The Ki values of SPC1 and SPC2 are 1.2 x 10(-7) and 4.0 x 10(-8) M, respectively. The complexes of SPC1 and SPC2 with bovine beta-trypsin (BTRY) were crystallized by ammonium sulphate precipitation at pH 6.4 and 6.0, respectively. The two crystals have the same crystal form with space group P2(1)2(1)2(1) and cell dimension of a = 63.2(2) A, b = 63.5(6) A, and c = 69.8(4) A. The crystal structure of one complex, SPC1-BTRY, was determined and refined at 2.2 A resolution to a final R-value of 19.2%. From the resulting electron density map, 9 residues of SPC1, from position 9I to 17I, were identified clearly and three-dimension atomic model of the 9-residue reactive loop formed by a disulfide bridge, Cys9I-Cys17I, was built. No electron density corresponding to the other 13 residues was observed in the present map.(ABSTRACT TRUNCATED AT 250 WORDS)
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20656696 R.T.Bradshaw, B.H.Patel, E.W.Tate, R.J.Leatherbarrow, and I.R.Gould (2011).
Comparing experimental and computational alanine scanning techniques for probing a prototypical protein-protein interaction.
  Protein Eng Des Sel, 24, 197-207.  
18850049 S.Wang, J.Han, Y.Wang, W.Lu, and C.Chi (2008).
Design of peptide inhibitors for furin based on the C-terminal fragment of histone H1.2.
  Acta Biochim Biophys Sin (Shanghai), 40, 848-854.  
  18084102 G.F.Esteves, R.C.Teles, N.S.Cavalcante, D.Neves, M.M.Ventura, J.A.Barbosa, and S.M.de Freitas (2007).
Crystallization, data collection and processing of the chymotrypsin-BTCI-trypsin ternary complex.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 1087-1090.  
17372355 M.Sherawat, P.Kaur, M.Perbandt, C.Betzel, W.A.Slusarchyk, G.S.Bisacchi, C.Chang, B.L.Jacobson, H.M.Einspahr, and T.P.Singh (2007).
Structure of the complex of trypsin with a highly potent synthetic inhibitor at 0.97 A resolution.
  Acta Crystallogr D Biol Crystallogr, 63, 500-507.
PDB code: 2ayw
15880256 R.F.Qi, Z.W.Song, and C.W.Chi (2005).
Structural features and molecular evolution of Bowman-Birk protease inhibitors and their potential application.
  Acta Biochim Biophys Sin (Shanghai), 37, 283-292.  
14501128 J.A.Barbosa, R.C.Teles, V.P.Forrer, B.G.Guimarães, F.J.Medrano, M.M.Ventura, and S.M.Freitas (2003).
Crystallization, data collection and phasing of black-eyed pea trypsin/chymotrypsin inhibitor in complex with bovine beta-trypsin.
  Acta Crystallogr D Biol Crystallogr, 59, 1828-1830.  
12186545 A.B.Brauer, G.J.Domingo, R.M.Cooke, S.J.Matthews, and R.J.Leatherbarrow (2002).
A conserved cis peptide bond is necessary for the activity of Bowman-Birk inhibitor protein.
  Biochemistry, 41, 10608-10615.  
11847280 A.Heifetz, E.Katchalski-Katzir, and M.Eisenstein (2002).
Electrostatics in protein-protein docking.
  Protein Sci, 11, 571-587.  
12325158 J.D.McBride, E.M.Watson, A.B.Brauer, A.M.Jaulent, and R.J.Leatherbarrow (2002).
Peptide mimics of the Bowman-Birk inhibitor reactive site loop.
  Biopolymers, 66, 79-92.  
11967374 M.Backovic, E.Stratikos, D.A.Lawrence, and P.G.Gettins (2002).
Structural similarity of the covalent complexes formed between the serpin plasminogen activator inhibitor-1 and the arginine-specific proteinases trypsin, LMW u-PA, HMW u-PA, and t-PA: use of site-specific fluorescent probes of local environment.
  Protein Sci, 11, 1182-1191.  
11257512 G.Zhu, Q.Huang, Y.Zhu, Y.Li, C.Chi, and Y.Tang (2001).
X-Ray study on an artificial mung bean inhibitor complex with bovine beta-trypsin in neat cyclohexane.
  Biochim Biophys Acta, 1546, 98.
PDB code: 1g9i
10944388 V.Z.Pletnev, T.S.Zamolodchikova, W.A.Pangborn, and W.L.Duax (2000).
Crystal structure of bovine duodenase, a serine protease, with dual trypsin and chymotrypsin-like specificities.
  Proteins, 41, 8.
PDB code: 1euf
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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