Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: Implications for the catalytic mechanism

Songsiriritthigul, Chomphunuch; Pantoom, Supansa; Aguda, A.H.; Robinson, Robert; Suginta, Wipa

doi:10.1016/j.jsb.2008.03.008

Cited by 71 publications

(83 citation statements)

References 51 publications

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“…This oligosaccharide bound in a small groove barely inside the barrel composing the middle of the enzyme, as shown in Figure 2(a). This agreed with literature, which reports the barrel as being the catalytic do-main of the enzyme [19,[33][34][35]. The active site of A. fumigatus CHIA1 is reported to contain Ala 124, Tyr125, Tyr232, Asn233, and Trp312 [19].…”

Section: Discussionsupporting

confidence: 90%

Blastomyces dermatitidis: Chitinase Homology Model, in Silico Docking, and Inhibition Assay

Searle¹,

Winston²,

Scalarone³

2012

OJMM

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Blastomyces dermatitidis is a thermally dimorphic fungus that causes the disease blastomycosis. Currently there are a limited number of effective treatments, many of which have harsh side effects. Chitin, a component of the fungal cell wall is often broken down and recycled for cell wall remodeling and growth. Chitinase is the digestive enzyme capable of chitin hydrolysis. By inhibiting the chitinase we predicted that cells wouldn't be able to divide and multiply normally, thereby leading to possible anti-fungal treatments. For this study we modeled the structure of B. dermatitidis chitinase, using homology modeling. By predicting a three-dimensional structure we were able to do additional analyses of the active site of the chitinase and predict the binding of a possible small molecule, acetazolamide, in silico. This binding allowed us to predict that this molecule might be capable of inhibiting the chitinase of B. dermatitidis. This inhibition was tested in vivo. No difference in the growth curves of the test and control organisms was observed, however there was a difference within the cell walls of the yeast cells. The cell walls appeared thicker with additional differences in cell wall orderly growth. These changes are consistent with changes that may occur as B. dermatitidis chitinases are inhibited.

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Section: Discussionsupporting

confidence: 90%

Blastomyces dermatitidis: Chitinase Homology Model, in Silico Docking, and Inhibition Assay

Searle¹,

Winston²,

Scalarone³

2012

OJMM

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“…This affinity gradient is supported by the B-factor being lowest for Ϫ2GlcNAc (43.63 Å 2 ), indicating high rigidity through tight interactions at the internal site. Increases in B-factor for bound sugar at the extending subsites (Ϫ1GlcNAc, 44 ) suggest greater flexibility of the sugar rings, which make weak interactions with the binding residues at such subsites.…”

Section: Resultsmentioning

confidence: 99%

Structural and Thermodynamic Insights into Chitooligosaccharide Binding to Human Cartilage Chitinase 3-like Protein 2 (CHI3L2 or YKL-39)

Ranok

Wongsantichon

Robinson

et al. 2015

Journal of Biological Chemistry

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Background: Human YKL-39 is currently recognized as a biomarker for osteoarthritis. Results: Crystal structures of YKL-39 reveal that chitooligosaccharide induces local conformational changes to stabilize sugar⅐protein complexes and that the protein contains five binding subsites for sugars. Conclusion: YKL-39 binds to chitooligosaccharide through enthalpic reactions. Significance: Our findings suggest how YKL-39 interacts with GlcNAc moieties of the natural ligands, which may possibly activate local tissue inflammation.

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“…2) (8,10,13,(35)(36)(37)(38)(39)(40)(41)(42)(43)(44). The sequences share several highly conserved fragments among all chitinases in which three regions are important.…”

Section: Resultsmentioning

confidence: 99%

Crystal Structures of Bacillus cereus NCTU2 Chitinase Complexes with Chitooligomers Reveal Novel Substrate Binding for Catalysis

Hsieh

Chiang

et al. 2010

Journal of Biological Chemistry

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Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: Implications for the catalytic mechanism

Cited by 71 publications

References 51 publications

<i>Blastomyces dermatitidis</i>: Chitinase Homology Model, <i>in Silico</i> Docking, and Inhibition Assay

<i>Blastomyces dermatitidis</i>: Chitinase Homology Model, <i>in Silico</i> Docking, and Inhibition Assay

Structural and Thermodynamic Insights into Chitooligosaccharide Binding to Human Cartilage Chitinase 3-like Protein 2 (CHI3L2 or YKL-39)

Crystal Structures of Bacillus cereus NCTU2 Chitinase Complexes with Chitooligomers Reveal Novel Substrate Binding for Catalysis

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Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: Implications for the catalytic mechanism

Cited by 71 publications

References 51 publications

&lt;i&gt;Blastomyces dermatitidis&lt;/i&gt;: Chitinase Homology Model, &lt;i&gt;in Silico&lt;/i&gt; Docking, and Inhibition Assay

&lt;i&gt;Blastomyces dermatitidis&lt;/i&gt;: Chitinase Homology Model, &lt;i&gt;in Silico&lt;/i&gt; Docking, and Inhibition Assay

Structural and Thermodynamic Insights into Chitooligosaccharide Binding to Human Cartilage Chitinase 3-like Protein 2 (CHI3L2 or YKL-39)

Crystal Structures of Bacillus cereus NCTU2 Chitinase Complexes with Chitooligomers Reveal Novel Substrate Binding for Catalysis

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<i>Blastomyces dermatitidis</i>: Chitinase Homology Model, <i>in Silico</i> Docking, and Inhibition Assay

<i>Blastomyces dermatitidis</i>: Chitinase Homology Model, <i>in Silico</i> Docking, and Inhibition Assay