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Hydrolase PDB-id
1dxj
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Protein chain
242 a.a. *
Ligands
SO4
Waters ×156

* Residue conservation analysis
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PDB id: 1dxj
Name: Hydrolase
Title: Structure of the chitinase from jack bean

Structure:
Class ii chitinase. Chain: a. Ec: 3.2.1.14

Source:
Canavalia ensiformis. Jack bean. Organism_taxid: 3823. Organ: seed

UniProt:
O81934 (O81934_CANEN) Pfam  
Seq:
Struc:
Seq: 270 a.a.
Struc: 242 a.a.
Key:    PfamA domain
 Secondary structure  CATH domain

Resolution:
1.8Å

R-factor:
0.182

R-free:
0.222

Authors:
M.Hahn,M.Hennig,B.Schlesier,W.Hohne

Key ref:
M.Hahn et al. (2000). Structure of jack bean chitinase.. Acta Crystallogr D Biol Crystallogr, 56, 1096-1099. [PubMed id: 10957628] [DOI: 10.1107/S090744490000857X]

Date:
10-Jan-00

Release date:
29-Aug-00

Related entries:
1cns crystal structure of chitinase at 1.91a resolution (endochitinase 2, ec 3.2.1.14)
1ctn chitinase a (E.C.3.2.1.14) (ph 5.5, 4 degrees c) from serratia marcescens
1d2k c. Immitis chitinase 1 at 2. 2 angstroms resolution
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    Key reference    
 
 
DOI no: 10.1107/S090744490000857X Acta Crystallogr D Biol Crystallogr 56:1096-1099 (2000)
PubMed id: 10957628  
 
 
Structure of jack bean chitinase.
M.Hahn, M.Hennig, B.Schlesier, W.Höhne.
 
  ABSTRACT  
 
The structure of jack bean chitinase was solved at 1.8 A resolution by molecular replacement. It is an alpha-helical protein with three disulfide bridges. The active site is related in structure to animal and viral lysozymes. However, unlike in lysozyme, the architecture of the active site suggests a single-step cleavage. According to this mechanism, Glu68 is the proton donor and Glu90 assists in the reaction by moving towards the substrate and recruiting a water molecule that acts as the nucleophile. In this model, a water molecule was found in contact with Glu90 O(epsilon1) and Thr119 O(gamma) at a distance of 3.0 and 2.8 A, respectively. The model is in accordance with the observed inversion mechanism.
 
  Selected figure(s)  
 
Figure 1.
Model of jack bean chitinase at 1.8 Å resolution. Helices and termini are indicated, disulfide bridges are identified by roman numerals (I, Cys24/Cys86; II, Cys98/Cys104; III, Cys203/Cys235). Glu68 is the catalytic residue in the cleavage reaction. Figs. 1 [link]-[turqarr.gif] and 3 [link]-[turqarr.gif] were drawn with MOLSCRIPT (Kraulis, 1991 [Kraulis, J. P. (1991). J. Appl. Cryst. 24, 946-950.]-[bluearr.gif] ).
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2000, 56, 1096-1099) copyright 2000.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19629717 W.Ubhayasekera, R.Rawat, S.W.Ho, M.Wiweger, S.Von Arnold, M.L.Chye, and S.L.Mowbray (2009).
The first crystal structures of a family 19 class IV chitinase: the enzyme from Norway spruce.
  Plant Mol Biol, 71, 277-289.  
17608716 W.Ubhayasekera, C.M.Tang, S.W.Ho, G.Berglund, T.Bergfors, M.L.Chye, and S.L.Mowbray (2007).
Crystal structures of a family 19 chitinase from Brassica juncea show flexibility of binding cleft loops.
  FEBS J, 274, 3695-3703.
PDB codes: 2z37 2z38 2z39
17010167 I.A.Hoell, B.Dalhus, E.B.Heggset, S.I.Aspmo, and V.G.Eijsink (2006).
Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes.
  FEBS J, 273, 4889-4900.
PDB code: 2cjl
16636468 T.Kawase, S.Yokokawa, A.Saito, T.Fujii, N.Nikaidou, K.Miyashita, and T.Watanabe (2006).
Comparison of enzymatic and antifungal properties between family 18 and 19 chitinases from S. coelicolor A3(2).
  Biosci Biotechnol Biochem, 70, 988-998.  
16279955 V.Seidl, B.Huemer, B.Seiboth, and C.P.Kubicek (2005).
A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases.
  FEBS J, 272, 5923-5939.  
14766598 T.Kawase, A.Saito, T.Sato, R.Kanai, T.Fujii, N.Nikaidou, K.Miyashita, and T.Watanabe (2004).
Distribution and phylogenetic analysis of family 19 chitinases in Actinobacteria.
  Appl Environ Microbiol, 70, 1135-1144.  
12755707 M.Ueda, M.Kojima, T.Yoshikawa, N.Mitsuda, K.Araki, T.Kawaguchi, K.Miyatake, M.Arai, and T.Fukamizo (2003).
A novel type of family 19 chitinase from Aeromonas sp. No.10S-24. Cloning, sequence, expression, and the enzymatic properties.
  Eur J Biochem, 270, 2513-2520.  
11999399 T.Ohnuma, M.Yagi, T.Yamagami, T.Taira, Y.Aso, and M.Ishiguro (2002).
Molecular cloning, functional expression, and mutagenesis of cDNA encoding rye (Secale cereale) seed chitinase-c.
  Biosci Biotechnol Biochem, 66, 277-284.  
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 codes are shown on the right.