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PDBsum entry 1d2k
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Hydrolase PDB id
1d2k

 

 

 

 

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Contents
Protein chain
392 a.a. *
Waters ×241
* Residue conservation analysis
PDB id:
1d2k
Name: Hydrolase
Title: C. Immitis chitinase 1 at 2.2 angstroms resolution
Structure: Chitinase 1. Chain: a. Fragment: residues 36-427. Engineered: yes
Source: Coccidioides immitis. Organism_taxid: 5501. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
2.20Å     R-factor:   0.170     R-free:   0.248
Authors: T.Hollis,A.F.Monzingo,K.Bortone,S.R.Ernst,R.Cox,J.D.Robertus
Key ref: T.Hollis et al. (2000). The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis. Protein Sci, 9, 544-551. PubMed id: 10752616 DOI: 10.1110/ps.9.3.544
Date:
23-Sep-99     Release date:   27-Sep-00    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0CB51  (CHI1_COCPS) -  Endochitinase 1 from Coccidioides posadasii (strain RMSCC 757 / Silveira)
Seq:
Struc: 		427 a.a.
392 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.14  - chitinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of the 1,4-beta-linkages of N-acetyl-D-glucosamine polymers of chitin.

 

 
DOI no: 10.1110/ps.9.3.544 Protein Sci 9:544-551 (2000)
PubMed id: 10752616  
 
 
The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis.
T.Hollis, A.F.Monzingo, K.Bortone, S.Ernst, R.Cox, J.D.Robertus.
 
  ABSTRACT  
 
The X-ray structure of chitinase from the fungal pathogen Coccidioides immitis has been solved to 2.2 A resolution. Like other members of the class 18 hydrolase family, this 427 residue protein is an eight-stranded beta/alpha-barrel. Although lacking an N-terminal chitin anchoring domain, the enzyme closely resembles the chitinase from Serratia marcescens. Among the conserved features are three cis peptide bonds, all involving conserved active site residues. The active site is formed from conserved residues such as tryptophans 47, 131, 315, 378, tyrosines 239 and 293, and arginines 52 and 295. Glu171 is the catalytic acid in the hydrolytic mechanism; it was mutated to a Gln, and activity was abolished. Allosamidin is a substrate analog that strongly inhibits the class 18 enzymes. Its binding to the chitinase hevamine has been observed, and we used conserved structural features of the two enzymes to predict the inhibitors binding to the fungal enzyme.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20084296 H.Li, and L.H.Greene (2010).
Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding.
  PLoS One, 5, e8654.  
20553502 H.Tsuji, S.Nishimura, T.Inui, Y.Kado, K.Ishikawa, T.Nakamura, and K.Uegaki (2010).
Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus- the role of conserved residues in the active site.
  FEBS J, 277, 2683-2695.
PDB codes: 3a4w 3a4x 3afb
  19342775 D.N.Patil, M.Datta, A.Chaudhary, S.Tomar, A.K.Sharma, and P.Kumar (2009).
Isolation, purification, crystallization and preliminary crystallographic studies of chitinase from tamarind (Tamarindus indica) seeds.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 343-345.  
19596709 M.Lienemann, H.Boer, A.Paananen, S.Cottaz, and A.Koivula (2009).
Toward understanding of carbohydrate binding and substrate specificity of a glycosyl hydrolase 18 family (GH-18) chitinase from Trichoderma harzianum.
  Glycobiology, 19, 1116-1126.  
18936994 V.N.Nguyen, I.J.Oh, Y.J.Kim, K.Y.Kim, Y.C.Kim, and R.D.Park (2009).
Purification and characterization of chitinases from Paecilomyces variotii DG-3 parasitizing on Meloidogyne incognita eggs.
  J Ind Microbiol Biotechnol, 36, 195-203.  
19568782 W.Suginta, S.Pantoom, and H.Prinz (2009).
Substrate binding modes and anomer selectivity of chitinase A from Vibrio harveyi.
  J Chem Biol, 2, 191-202.  
19420714 Y.Takenaka, S.Nakano, M.Tamoi, S.Sakuda, and T.Fukamizo (2009).
Chitinase gene expression in response to environmental stresses in Arabidopsis thaliana: chitinase inhibitor allosamidin enhances stress tolerance.
  Biosci Biotechnol Biochem, 73, 1066-1071.  
18680214 C.Petter, C.Scholz, H.Wessner, G.Hansen, P.Henklein, T.Watanabe, and W.Höhne (2008).
Phage display screening for peptidic chitinase inhibitors.
  J Mol Recognit, 21, 401-409.  
18397326 H.H.Chuang, H.Y.Lin, and F.P.Lin (2008).
Biochemical characteristics of C-terminal region of recombinant chitinase from Bacillus licheniformis: implication of necessity for enzyme properties.
  FEBS J, 275, 2240-2254.  
17543889 Zaheer-ul-Haq, P.Dalal, N.N.Aronson, and J.D.Madura (2007).
Family 18 chitolectins: comparison of MGP40 and HUMGP39.
  Biochem Biophys Res Commun, 359, 221-226.  
16761182 L.Duo-Chuan (2006).
Review of fungal chitinases.
  Mycopathologia, 161, 345-360.  
16428843 N.N.Aronson, B.A.Halloran, M.F.Alexeyev, X.E.Zhou, Y.Wang, E.J.Meehan, and L.Chen (2006).
Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation.
  Biosci Biotechnol Biochem, 70, 243-251.
PDB code: 1rd6
16420473 S.J.Horn, A.Sørbotten, B.Synstad, P.Sikorski, M.Sørlie, K.M.Vårum, and V.G.Eijsink (2006).
Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens.
  FEBS J, 273, 491-503.  
16487309 S.M.Bonfim, A.H.Cruz, R.S.Jesuino, C.J.Ulhoa, E.E.Molinari-Madlum, C.M.Soares, and M.Pereira (2006).
Chitinase from Paracoccidioides brasiliensis: molecular cloning, structural, phylogenetic, expression and activity analysis.
  FEMS Immunol Med Microbiol, 46, 269-283.  
16193156 O.A.Andersen, M.J.Dixon, I.M.Eggleston, and D.M.van Aalten (2005).
Natural product family 18 chitinase inhibitors.
  Nat Prod Rep, 22, 563-579.  
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.  
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.  
15103145 H.Hu, G.Wang, H.Yang, J.Zhou, L.Mo, K.Yang, C.Jin, C.Jin, and Z.Rao (2004).
Crystallization and preliminary crystallographic analysis of a native chitinase from the fungal pathogen Aspergillus fumigatus YJ-407.
  Acta Crystallogr D Biol Crystallogr, 60, 939-940.  
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.  
12554965 Y.Papanikolau, G.Tavlas, C.E.Vorgias, and K.Petratos (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.
PDB codes: 1edq 1ffq
11481469 D.M.van Aalten, D.Komander, B.Synstad, S.Gåseidnes, M.G.Peter, and V.G.Eijsink (2001).
Structural insights into the catalytic mechanism of a family 18 exo-chitinase.
  Proc Natl Acad Sci U S A, 98, 8979-8984.
PDB codes: 1e6n 1e6p 1e6r 1e6z
11327866 T.Fukamizo, C.Sasaki, E.Schelp, K.Bortone, and J.D.Robertus (2001).
Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis.
  Biochemistry, 40, 2448-2454.  
11160110 T.Lonhienne, K.Mavromatis, C.E.Vorgias, L.Buchon, C.Gerday, and V.Bouriotis (2001).
Cloning, sequences, and characterization of two chitinase genes from the Antarctic Arthrobacter sp. strain TAD20: isolation and partial characterization of the enzymes.
  J Bacteriol, 183, 1773-1779.  
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.

 

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