title: Structural investigation of a novel N-acetyl glucosamine binding chi-lectin which reveals evolutionary relationship with class III chitinases.
abstract: The glycosyl hydrolase 18 (GH18) family consists of active chitinases as well as chitinase like lectins/proteins (CLPs). The CLPs share significant sequence and structural similarities with active chitinases, however, do not display chitinase activity. Some of these proteins are reported to have specific functions and carbohydrate binding property. In the present study, we report a novel chitinase like lectin (TCLL) from Tamarindus indica. The crystal structures of native TCLL and its complex with N-acetyl glucosamine were determined. Similar to the other CLPs of the GH18 members, TCLL lacks chitinase activity due to mutations of key active site residues. Comparison of TCLL with chitinases and other chitin binding CLPs shows that TCLL has substitution of some chitin binding site residues and more open binding cleft due to major differences in the loop region. Interestingly, the biochemical studies suggest that TCLL is an N-acetyl glucosamine specific chi-lectin, which is further confirmed by the complex structure of TCLL with N-acetyl glucosamine complex. TCLL has two distinct N-acetyl glucosamine binding sites S1 and S2 that contain similar polar residues, although interaction pattern with N-acetyl glucosamine varies extensively among them. Moreover, TCLL structure depicts that how plants utilize existing structural scaffolds ingenuously to attain new functions. To date, this is the first structural investigation of a chi-lectin from plants that explore novel carbohydrate binding sites other than chitin binding groove observed in GH18 family members. Consequently, TCLL structure confers evidence for evolutionary link of lectins with chitinases.
authors.affiliation: Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, India.
authors.forename: Dipak N
authors.initials: DN
authors.lastname: Patil
authors.forename: Manali
authors.initials: M
authors.lastname: Datta
authors.forename: Aditya
authors.initials: A
authors.lastname: Dev
authors.forename: Sonali
authors.initials: S
authors.lastname: Dhindwal
authors.forename: Nirpendra
authors.initials: N
authors.lastname: Singh
authors.forename: Pushpanjali
authors.initials: P
authors.lastname: Dasauni
authors.forename: Suman
authors.initials: S
authors.lastname: Kundu
authors.forename: Ashwani K
authors.initials: AK
authors.lastname: Sharma
authors.forename: Shailly
authors.initials: S
authors.lastname: Tomar
authors.forename: Pravindra
authors.initials: P
authors.lastname: Kumar
mesh_terms: D000117:Acetylglucosamine / Q000737:chemistry; D000595:Amino Acid Sequence; D020134:Catalytic Domain; D002688:Chitinases / Q000737:chemistry* / Q000494:pharmacology; D018360:Crystallography, X-Ray; D019143:Evolution, Molecular; D006384:Hemagglutination; D006388:Hemagglutinins / Q000737:chemistry* / Q000494:pharmacology; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010802:Phylogeny; D037121:Plant Lectins / Q000737:chemistry* / Q000494:pharmacology; D010940:Plant Proteins / Q000737:chemistry* / Q000494:pharmacology; D011485:Protein Binding; D020539:Sequence Analysis, Protein; D040681:Structural Homology, Protein; D029861:Tamarindus / Q000201:enzymology*
chemical_list: D006388:Hemagglutinins; D037121:Plant Lectins; D010940:Plant Proteins; D002688:Chitinases; C110892:chitinase, class III; D000117:Acetylglucosamine