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Hydrolase PDB id
1edq
Jmol
Contents
Protein chain
540 a.a. *
Waters ×909
* Residue conservation analysis
PDB id:
1edq
Name: Hydrolase
Title: Crystal structure of chitinase a from s. Marcescens at 1.55 angstroms
Structure: Chitinase a. Chain: a. Engineered: yes
Source: Serratia marcescens. Organism_taxid: 615. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
1.55Å     R-factor:   0.188     R-free:   0.215
Authors: Y.Papanikolau,K.Petratos
Key ref:
Y.Papanikolau et al. (2003). De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin. Acta Crystallogr D Biol Crystallogr, 59, 400-403. PubMed id: 12554965 DOI: 10.1107/S0907444902021923
Date:
28-Jan-00     Release date:   18-Feb-00    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O83008  (O83008_SERMA) -  Chitinase A (Precursor)
Seq:
Struc: 		 
Seq:
Struc: 		563 a.a.
540 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   3 terms 
  Biochemical function     catalytic activity     6 terms  

 

 
DOI no: 10.1107/S0907444902021923 Acta Crystallogr D Biol Crystallogr 59:400-403 (2003)
PubMed id: 12554965  
 
 
De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin.
Y.Papanikolau, G.Tavlas, C.E.Vorgias, K.Petratos.
 
  ABSTRACT  
 
The purification scheme of chitinase A (ChiA) from S. marcescens has been extensively revised. The pure enzyme crystallizes readily under new crystallization conditions. The ChiA crystal structure has been refined to 1.55 A resolution and the crystal structure of ChiA co-crystallized with the inhibitor allosamidin has been refined to 1.9 A resolution. Allosamidin is located in the deep active-site tunnel of ChiA and interacts with three important residues: Glu315, the proton donor of the catalysis, Asp313, which adopts two conformations in the native structure but is oriented towards Glu315 in the inhibitor complex, and Tyr390, which lies opposite Glu315 in the active-site tunnel.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 ChiA-allosamidin complex. (a) Stereoview of the C^ -atom trace of the enzyme molecule (green) with the inhibitor (red) bound to the active-site tunnel (PDB code [112]1ffq ). (b) Allosamidin in the electron density of the weighted 2F[o] - F[c] map contoured at 2 [113][sigma] (blue) and the neighbouring residues of ChiA. (c) Close-up view of allosamidin bound to the enzyme's active-site tunnel at subsites -1 to -3. The allosamizoline moiety fits into a local well.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 400-403) copyright 2003.  
  Figure was selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20361049 J.O.Wrabl, and V.J.Hilser (2010).
Investigating homology between proteins using energetic profiles.
  PLoS Comput Biol, 6, e1000722.  
20829286 J.Yang, Z.Gan, Z.Lou, N.Tao, Q.Mi, L.Liang, Y.Sun, Y.Guo, X.Huang, C.Zou, Z.Rao, Z.Meng, and K.Q.Zhang (2010).
Crystal structure and mutagenesis analysis of chitinase CrChi1 from the nematophagous fungus Clonostachys rosea in complex with the inhibitor caffeine.
  Microbiology, 156, 3566-3574.
PDB codes: 3g6l 3g6m
16685709 S.Pyrpassopoulos, M.Vlassi, A.Tsortos, Y.Papanikolau, K.Petratos, C.E.Vorgias, and G.Nounesis (2006).
Equilibrium heat-induced denaturation of chitinase 40 from Streptomyces thermoviolaceus.
  Proteins, 64, 513-523.  
16183021 F.V.Rao, O.A.Andersen, K.A.Vora, J.A.Demartino, and D.M.van Aalten (2005).
Methylxanthine drugs are chitinase inhibitors: investigation of inhibition and binding modes.
  Chem Biol, 12, 973-980.
PDB codes: 2a3a 2a3b 2a3c 2a3e
14717693 B.Synstad, S.Gåseidnes, D.M.Van Aalten, G.Vriend, J.E.Nielsen, and V.G.Eijsink (2004).
Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase.
  Eur J Biochem, 271, 253-262.  
14597613 G.Vaaje-Kolstad, A.Vasella, M.G.Peter, C.Netter, D.R.Houston, B.Westereng, B.Synstad, V.G.Eijsink, and D.M.van Aalten (2004).
Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-delta-lactone.
  J Biol Chem, 279, 3612-3619.
PDB codes: 1ur8 1ur9
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