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PDBsum entry 1nh6

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protein ligands links
Hydrolase PDB id
1nh6
Jmol
Contents
Protein chain
540 a.a. *
Ligands
NAG-NAG-NAG-NAG-
NAG-NAG
Waters ×635
* Residue conservation analysis
PDB id:
1nh6
Name: Hydrolase
Title: Structure of s. Marcescens chitinase a, e315l, complex with hexasaccharide
Structure: Chitinase a. Chain: a. Engineered: yes. Mutation: yes
Source: Serratia marcescens. Organism_taxid: 615. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.05Å     R-factor:   0.197     R-free:   0.227
Authors: N.N.Aronson Jr.,B.A.Halloran,M.F.Alexyev,L.Amable,J.D.Madura L.Pasupulati,C.Worth,P.Van Roey
Key ref: N.N.Aronson et al. (2003). Family 18 chitinase-oligosaccharide substrate interaction: subsite preference and anomer selectivity of Serratia marcescens chitinase A. Biochem J, 376, 87-95. PubMed id: 12932195
Date:
18-Dec-02     Release date:   18-Mar-03    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07254  (CHIA_SERMA) -  Chitinase A
Seq:
Struc:
 
Seq:
Struc:
563 a.a.
540 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 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.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   4 terms 
  Biochemical function     hydrolase activity     4 terms  

 

 
Biochem J 376:87-95 (2003)
PubMed id: 12932195  
 
 
Family 18 chitinase-oligosaccharide substrate interaction: subsite preference and anomer selectivity of Serratia marcescens chitinase A.
N.N.Aronson, B.A.Halloran, M.F.Alexyev, L.Amable, J.D.Madura, L.Pasupulati, C.Worth, P.Van Roey.
 
  ABSTRACT  
 
The sizes and anomers of the products formed during the hydrolysis of chitin oligosaccharides by the Family 18 chitinase A (ChiA) from Serratia marcescens were analysed by hydrophilic interaction chromatography using a novel approach in which reactions were performed at 0 degrees C to stabilize the anomer conformations of the initial products. Crystallographic studies of the enzyme, having the structure of the complex of the ChiA E315L (Glu315-->Leu) mutant with a hexasaccharide, show that the oligosaccharide occupies subsites -4 to +2 in the substrate-binding cleft, consistent with the processing of beta-chitin by the release of disaccharide at the reducing end. Products of the hydrolysis of hexa- and penta-saccharides by wild-type ChiA, as well as by two mutants of the residues Trp275 and Phe396 important in binding the substrate at the +1 and +2 sites, show that the substrates only occupy sites -2 to +2 and that additional N -acetyl-D-glucosamines extend beyond the substrate-binding cleft at the reducing end. The subsites -3 and -4 are not used in this four-site binding mode. The explanation for these results is found in the high importance of individual binding sites for the processing of short oligosaccharides compared with the cumulative recognition and processive hydrolysis mechanism used to digest natural beta-chitin.
 

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.  
20559489 J.Kumirska, M.Czerwicka, Z.KaczyƄski, A.Bychowska, K.Brzozowski, J.Thöming, and P.Stepnowski (2010).
Application of spectroscopic methods for structural analysis of chitin and chitosan.
  Mar Drugs, 8, 1567-1636.  
19244232 H.Zakariassen, B.B.Aam, S.J.Horn, K.M.Vårum, M.Sørlie, and V.G.Eijsink (2009).
Aromatic Residues in the Catalytic Center of Chitinase A from Serratia marcescens Affect Processivity, Enzyme Activity, and Biomass Converting Efficiency.
  J Biol Chem, 284, 10610-10617.  
19307719 P.Sharma, N.Singh, M.Sinha, S.Sharma, M.Perbandt, C.Betzel, P.Kaur, A.Srinivasan, and T.P.Singh (2009).
Tryptophan as a three-way switch in regulating the function of the secretory signalling glycoprotein (SPS-40) from mammary glands: structure of SPS-40 complexed with 2-methylpentane-2,4-diol at 1.6 A resolution.
  Acta Crystallogr D Biol Crystallogr, 65, 375-378.
PDB code: 2pi6
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.  
17372347 J.Kumar, A.S.Ethayathulla, D.B.Srivastava, N.Singh, S.Sharma, P.Kaur, A.Srinivasan, and T.P.Singh (2007).
Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40) and its functional implications: structures of the native glycoprotein and its four complexes with chitin-like oligosaccharides.
  Acta Crystallogr D Biol Crystallogr, 63, 437-446.
PDB codes: 2dsz 2dt0 2dt1 2dt2 2dt3
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
16269803 Q.Li, F.Wang, Y.Zhou, and X.Xiao (2005).
Putative exposed aromatic and hydroxyl residues on the surface of the N-terminal domains of Chi1 from Aeromonas caviae CB101 are essential for chitin binding and hydrolysis.
  Appl Environ Microbiol, 71, 7559-7561.  
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.