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PDBsum entry 1mct

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protein metals Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
1mct

 

 

 

 

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Contents
Protein chains
223 a.a. *
28 a.a. *
Metals
_CA
Waters ×405
* Residue conservation analysis
PDB id:
1mct
Name: Hydrolase/hydrolase inhibitor
Title: The refined 1.6 angstroms resolution crystal structure of the complex formed between porcine beta-trypsin and mcti-a, a trypsin inhibitor of squash family
Structure: Beta-trypsin. Chain: a. Engineered: yes. Trypsin inhibitor a. Chain: i. Engineered: yes
Source: Sus scrofa. Pig. Organism_taxid: 9823. Organ: seed. Momordica charantia. Balsam pear. Organism_taxid: 3673. Organ: seed
Biol. unit: Tetramer (from PQS)
Resolution:
1.60Å     R-factor:   0.167    
Authors: Q.Huang,S.Liu,Y.Tang
Key ref: Q.Huang et al. (1993). Refined 1.6 A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex. J Mol Biol, 229, 1022-1036. PubMed id: 8445634
Date:
24-Oct-92     Release date:   31-Jan-94    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00761  (TRYP_PIG) -  Trypsin from Sus scrofa
Seq:
Struc:
231 a.a.
223 a.a.*
Protein chain
Pfam   ArchSchema ?
P30709  (ITRA_MOMCH) -  Trypsin inhibitor A from Momordica charantia
Seq:
Struc:
28 a.a.
28 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

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

 

 
J Mol Biol 229:1022-1036 (1993)
PubMed id: 8445634  
 
 
Refined 1.6 A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex.
Q.Huang, S.Liu, Y.Tang.
 
  ABSTRACT  
 
The crystal structure of the complex formed by porcine beta-trypsin with the MCTI-A inhibitor (Momordica charantia, Linn. Cucurbitaceae) has been determined at 1.6 A resolution using the molecular replacement method. The sequence of MCTI-A was determined by recognizing the electron density, and shows that MCTI-A is a member of the squash family of trypsin inhibitors. We report the first high-resolution structure of porcine beta-trypsin. Detailed comparisons have been made on the overall structure, solvent structure and active-site geometries between this complex and bovine beta-trypsin and its complexes. On the basis of our results, we discuss the interaction patterns between inhibitor and trypsin. Unlike other complex structures formed by bovine trypsin with inhibitors, no out-of-plane distortion around the inhibitor's scissible peptide was observed. The role of the trypsin catalytic triad is also discussed on the basis of this structure.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21116528 Y.Zhou, and Y.Zhang (2011).
Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate.
  Chem Commun (Camb), 47, 1577-1579.  
19077275 A.Heitz, O.Avrutina, D.Le-Nguyen, U.Diederichsen, J.F.Hernandez, J.Gracy, H.Kolmar, and L.Chiche (2008).
Knottin cyclization: Impact on Structure and Dynamics.
  BMC Struct Biol, 8, 54.  
18004751 J.W.Torrance, M.W.Macarthur, and J.M.Thornton (2008).
Evolution of binding sites for zinc and calcium ions playing structural roles.
  Proteins, 71, 813-830.  
10842337 A.A.Gorfe, B.O.Brandsdal, H.K.Leiros, R.Helland, and A.O.Smalås (2000).
Electrostatics of mesophilic and psychrophilic trypsin isoenzymes: qualitative evaluation of electrostatic differences at the substrate binding site.
  Proteins, 40, 207-217.  
10672012 H.K.Leiros, N.P.Willassen, and A.O.Smalås (2000).
Structural comparison of psychrophilic and mesophilic trypsins. Elucidating the molecular basis of cold-adaptation.
  Eur J Biochem, 267, 1039-1049.  
11004551 K.Kamei, S.Sato, N.Hamato, R.Takano, K.Ohshima, R.Yamamoto, T.Nishino, H.Kato, and S.Hara (2000).
Effect of P(2)' site tryptophan and P(20)' site deletion of Momordica charantia trypsin inhibitor II on inhibition of proteinases.
  Biochim Biophys Acta, 1480, 6.  
10026173 H.M.Murthy, S.Clum, and R.Padmanabhan (1999).
Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects.
  J Biol Chem, 274, 5573-5580.
PDB code: 1bef
10089404 R.Helland, G.I.Berglund, J.Otlewski, W.Apostoluk, O.A.Andersen, N.P.Willassen, and A.O.Smalås (1999).
High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes.
  Acta Crystallogr D Biol Crystallogr, 55, 139-148.
PDB codes: 2btc 2sta 2stb
10531473 R.Recacha, M.Carson, M.J.Costanzo, B.Maryanoff, L.J.DeLucas, and D.Chattopadhyay (1999).
Structure of the RWJ-51084-bovine pancreatic beta-trypsin complex at 1.8 A.
  Acta Crystallogr D Biol Crystallogr, 55, 1785-1791.
PDB code: 1qcp
9242660 M.T.Stubbs, R.Morenweiser, J.Stürzebecher, M.Bauer, W.Bode, R.Huber, G.P.Piechottka, G.Matschiner, C.P.Sommerhoff, H.Fritz, and E.A.Auerswald (1997).
The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition.
  J Biol Chem, 272, 19931-19937.
PDB code: 1ldt
9384562 S.Di Marco, and J.P.Priestle (1997).
Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LDTI-tryptase system.
  Structure, 5, 1465-1474.
PDB code: 1an1
7716167 J.Janin (1995).
Elusive affinities.
  Proteins, 21, 30-39.  
7552703 S.L.Lin, and R.Nussinov (1995).
A disulphide-reinforced structural scaffold shared by small proteins with diverse functions.
  Nat Struct Biol, 2, 835-837.  
7846025 A.O.Smalås, E.S.Heimstad, A.Hordvik, N.P.Willassen, and R.Male (1994).
Cold adaption of enzymes: structural comparison between salmon and bovine trypsins.
  Proteins, 20, 149-166.
PDB code: 2tbs
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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