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

 

 

 

 

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Contents
Protein chain
223 a.a. *
Ligands
ACE-LEU-LEU-AR7
Metals
_CA
Waters ×510
* Residue conservation analysis
PDB id:
1jrs
Name: Hydrolase/hydrolase inhibitor
Title: Hemiacetal complex between leupeptin and trypsin
Structure: Trypsin. Chain: a. Leupeptin. Chain: b. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Synthetic: yes. Actinomycetes streptomyces roseus ma 839-a1. Organism_taxid: 66430
Biol. unit: Dimer (from PQS)
Resolution:
1.80Å     R-factor:   0.175     R-free:   0.207
Authors: I.V.Kurinov,R.W.Harrison
Key ref: I.V.Kurinov and R.W.Harrison (1996). Two crystal structures of the leupeptin-trypsin complex. Protein Sci, 5, 752-758. PubMed id: 8845765 DOI: 10.1002/pro.5560050420
Date:
07-Feb-96     Release date:   14-Oct-96    
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.

 

 
DOI no: 10.1002/pro.5560050420 Protein Sci 5:752-758 (1996)
PubMed id: 8845765  
 
 
Two crystal structures of the leupeptin-trypsin complex.
I.V.Kurinov, R.W.Harrison.
 
  ABSTRACT  
 
Three-dimensional structures of trypsin with the reversible inhibitor leupeptin have been determined in two different crystal forms. The first structure was determined at 1.7 A resolution with R-factor = 17.7% in the trigonal crystal space group P3(1)21, with unit cell dimensions of a = b = 55.62 A, c = 110.51 A. The second structure was determined at a resolution of 1.8 A with R-factor = 17.5% in the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions of a = 63.69 A, b = 69.37 A, c = 63.01 A. The overall protein structure is very similar in both crystal forms, with RMS difference for main-chain atoms of 0.27 A. The leupeptin backbone forms four hydrogen bonds with trypsin and a fifth hydrogen bond interaction is mediated by a water molecule. The aldehyde carbonyl of leupeptin forms a covalent bond of 1.42 A length with side-chain oxygen of Ser-195 in the active site. The reaction of trypsin with leupeptin proceeds through the formation of stable tetrahedral complex in which the hemiacetal oxygen atom is pointing out of the oxyanion hole and forming a hydrogen bond with His-57.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
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
16636277 E.S.Radisky, J.M.Lee, C.J.Lu, and D.E.Koshland (2006).
Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates.
  Proc Natl Acad Sci U S A, 103, 6835-6840.
PDB codes: 2age 2agg 2agi 2ah4
11327865 D.Neidhart, Y.Wei, C.Cassidy, J.Lin, W.W.Cleland, and P.A.Frey (2001).
Correlation of low-barrier hydrogen bonding and oxyanion binding in transition state analogue complexes of chymotrypsin.
  Biochemistry, 40, 2439-2447.
PDB codes: 1gg6 1ggd
11602025 S.Bhattacharya, S.Ghosh, S.Chakraborty, A.K.Bera, B.P.Mukhopadhayay, I.Dey, and A.Banerjee (2001).
Insight to structural subsite recognition in plant thiol protease-inhibitor complexes : understanding the basis of differential inhibition and the role of water.
  BMC Struct Biol, 1, 4.  
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
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
9109667 C.S.Cassidy, J.Lin, and P.A.Frey (1997).
A new concept for the mechanism of action of chymotrypsin: the role of the low-barrier hydrogen bond.
  Biochemistry, 36, 4576-4584.  
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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