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PDBsum entry 1nh6
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Structure of s. Marcescens chitinase a, e315l, complex with hexasaccharide
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Structure:
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Chitinase a. Chain: a. Engineered: yes. Mutation: yes
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Source:
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Serratia marcescens. Organism_taxid: 615. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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2.05Å
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R-factor:
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0.197
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R-free:
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0.227
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Authors:
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N.N.Aronson Jr.,B.A.Halloran,M.F.Alexyev,L.Amable,J.D.Madura, L.Pasupulati,C.Worth,P.Van Roey
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Key ref:
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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:
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Date:
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18-Dec-02
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Release date:
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18-Mar-03
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PROCHECK
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Headers
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References
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P07254
(CHIA_SERMA) -
Chitinase A from Serratia marcescens
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Seq:
Struc:
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563 a.a.
540 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 8 residue positions (black
crosses)
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Enzyme class:
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E.C.3.2.1.14
- chitinase.
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Reaction:
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Hydrolysis of the 1,4-beta-linkages of N-acetyl-D-glucosamine polymers of chitin.
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Biochem J
376:87-95
(2003)
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PubMed id:
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Family 18 chitinase-oligosaccharide substrate interaction: subsite preference and anomer selectivity of Serratia marcescens chitinase A.
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N.N.Aronson,
B.A.Halloran,
M.F.Alexyev,
L.Amable,
J.D.Madura,
L.Pasupulati,
C.Worth,
P.Van Roey.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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H.Li,
and
L.H.Greene
(2010).
Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding.
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PLoS One,
5,
e8654.
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J.Kumirska,
M.Czerwicka,
Z.Kaczyński,
A.Bychowska,
K.Brzozowski,
J.Thöming,
and
P.Stepnowski
(2010).
Application of spectroscopic methods for structural analysis of chitin and chitosan.
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Mar Drugs,
8,
1567-1636.
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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.
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J Biol Chem,
284,
10610-10617.
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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.
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Acta Crystallogr D Biol Crystallogr,
65,
375-378.
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PDB code:
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W.Suginta,
S.Pantoom,
and
H.Prinz
(2009).
Substrate binding modes and anomer selectivity of chitinase A from Vibrio harveyi.
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J Chem Biol,
2,
191-202.
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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.
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Acta Crystallogr D Biol Crystallogr,
63,
437-446.
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PDB codes:
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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.
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FEBS J,
273,
4889-4900.
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PDB code:
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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.
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Appl Environ Microbiol,
71,
7559-7561.
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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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Links
