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Hydrolase (serine proteinase) PDB-id
1tab
Asymmetric unit
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Contents
Description
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Protein chains
223 a.a. *
36 a.a. *
Waters ×140

* Residue conservation analysis
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  Biological unit*, tetramer
(*as deduced by PQS)
PDB id: 1tab
Name: Hydrolase (serine proteinase)
Title: Structure of the trypsin-binding domain of bowman-birk type protease inhibitor and its interaction with trypsin

Structure:
Trypsin. Chain: e. Engineered: yes. Bowman-birk type proteinase inhibitor. Chain: i. Engineered: yes

Source:
Bos taurus. Cow. Organism_taxid: 9913. Tissue: pancreas.

Biological unit:
Tetramer (from PQS)

UniProt:
Chain E: P00760 (TRY1_BOVIN)
Pfam   ArchSchema ?
Seq: 246 a.a.
Struc: 223 a.a.

Chain I: P01058 (IBB1_PHAAN)
Pfam   ArchSchema ?
Seq: 82 a.a.
Struc: 36 a.a.*
Key:    PfamA domain
 Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Enzyme class:
Chain E: E.C.3.4.21.4   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

Resolution:
2.30Å

R-factor:
0.200

Authors:
Y.Tsunogae,I.Tanaka,T.Yamane,J.-I.Kikkawa,T.Ashida, C.Ishikawa,K.Watanabe,S.Nakamura,K.Takahashi

Key ref:
Y.Tsunogae et al. (1986). Structure of the trypsin-binding domain of Bowman-Birk type protease inhibitor and its interaction with trypsin.. J Biochem (tokyo), 100, 1637-1646. [PubMed id: 3032921]

Date:
15-Oct-90

Release date:
15-Jan-92
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    Key reference    
 
 
J Biochem (tokyo) 100:1637-1646 (1986)
PubMed id: 3032921  
 
 
Structure of the trypsin-binding domain of Bowman-Birk type protease inhibitor and its interaction with trypsin.
Y.Tsunogae, I.Tanaka, T.Yamane, J.Kikkawa, T.Ashida, C.Ishikawa, K.Watanabe, S.Nakamura, K.Takahashi.
 
  ABSTRACT  
 
The crystal structure of the complex formed by bovine trypsin and Bowman-Birk type protease inhibitor AB-I extracted from azuki beans (Vigna angularis) 'Takara' has been analyzed. The structure was solved by the application of the phase combination of single isomorphous phases and trypsin model phases, followed by phase improvement using the iterative Fourier technique. From the resulting electron density map, a three-dimensional atomic model of the trypsin binding domain of AB-I has been built. The peptide chain at the trypsin reactive site turns back sharply at Pro29 and forms a 9-residue ring (Cys24-Cys32). The 'front side' of this ring, consisting of the reactive site (Cys24-Met28), interacts with trypsin in a similar manner to other families of inhibitors and forms a stable complex, which seems to be maintained by the interactions with the 'back side' of this ring (Pro29-Cys34). The similar spatial arrangements of the 'back side' of this inhibitor and the 'secondary contact region' of the other inhibitors with respect to the reactive site suggest an important common role of these regions in exhibiting inhibitory activity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  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.  
17142290 J.A.Barbosa, L.P.Silva, R.C.Teles, G.F.Esteves, R.B.Azevedo, M.M.Ventura, and S.M.de Freitas (2007).
Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases.
  Biophys J, 92, 1638-1650.
PDB code: 2g81
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.  
12931008 J.R.Bradford, and D.R.Westhead (2003).
Asymmetric mutation rates at enzyme-inhibitor interfaces: implications for the protein-protein docking problem.
  Protein Sci, 12, 2099-2103.  
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.  
12112698 F.R.Melo, D.J.Rigden, O.L.Franco, L.V.Mello, M.B.Ary, M.F.Grossi de Sá, and C.Bloch (2002).
Inhibition of trypsin by cowpea thionin: characterization, molecular modeling, and docking.
  Proteins, 48, 311-319.  
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.  
  10452608 D.J.Sloan, and H.W.Hellinga (1999).
Dissection of the protein G B1 domain binding site for human IgG Fc fragment.
  Protein Sci, 8, 1643-1648.  
10393310 H.M.Krishna Murthy, K.Judge, L.DeLucas, S.Clum, and R.Padmanabhan (1999).
Crystallization, characterization and measurement of MAD data on crystals of dengue virus NS3 serine protease complexed with mung-bean Bowman-Birk inhibitor.
  Acta Crystallogr D Biol Crystallogr, 55, 1370-1372.  
10531495 K.N.Rao, S.S.Hegde, R.J.Lewis, and C.G.Suresh (1999).
Crystallization and preliminary x-ray diffraction studies of a Bowman-Birk inhibitor from Vigna unguiculata seeds.
  Acta Crystallogr D Biol Crystallogr, 55, 1920-1922.  
10329799 Y.S.Kim, H.K.Song, and S.W.Suh (1999).
Crystallization and preliminary X-ray analysis of a complex between the Bowman-Birk trypsin inhibitor from barley and porcine pancreatic trypsin.
  Acta Crystallogr D Biol Crystallogr, 55, 1244-1246.  
9761922 H.K.Song, and S.W.Suh (1998).
Preliminary X-ray crystallographic analysis of Bowman-Birk trypsin inhibitor from barley seeds.
  Acta Crystallogr D Biol Crystallogr, 54, 441-443.  
8895102 A.S.Tanaka, M.U.Sampaio, R.Mentele, E.A.Auerswald, and C.A.Sampaio (1996).
Sequence of a new Bowman-Birk inhibitor from Torresea acreana seeds and comparison with Torresea cearensis trypsin inhibitor (TcTI2).
  J Protein Chem, 15, 553-560.  
8662008 B.Prakash, S.Selvaraj, M.R.Murthy, Y.N.Sreerama, D.R.Rao, and L.R.Gowda (1996).
Analysis of the amino acid sequences of plant Bowman-Birk inhibitors.
  J Mol Evol, 42, 560-569.  
8552589 S.Jones, and J.M.Thornton (1996).
Principles of protein-protein interactions.
  Proc Natl Acad Sci U S A, 93, 13-20.  
7656006 H.A.Schreuder, B.de Boer, R.Dijkema, J.Mulders, H.J.Theunissen, P.D.Grootenhuis, and W.G.Hol (1994).
The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions.
  Nat Struct Biol, 1, 48-54.
PDB code: 1ath
1584773 Y.Takeuchi, T.Nonaka, K.T.Nakamura, S.Kojima, K.Miura, and Y.Mitsui (1992).
Crystal structure of an engineered subtilisin inhibitor complexed with bovine trypsin.
  Proc Natl Acad Sci U S A, 89, 4407-4411.
PDB code: 2tld
2096886 P.Ascenzi, G.Amiconi, M.Bolognesi, E.Menegatti, and M.Guarneri (1990).
Binding of the soybean Bowman-Birk proteinase inhibitor and of its chymotrypsin and trypsin inhibiting fragments to bovine alpha-chymotrypsin and bovine beta-trypsin. A thermodynamic study.
  J Mol Recognit, 3, 192-196.  
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.