4nzc

Crystal structure of Chitinase D from Serratia proteamaculans at 1.45 Angstrom resolution

spinqualitylabelsall models 4nzc, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nzc is a 1 chain structure with sequence from Serratia proteamaculans 568. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: ACT, GOL, OMT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A8GFD6_SERP5 Publication Abstract from PubMed Chitinases are known to hydrolyze chitin polymers into smaller chitooligosaccharides. Chitinase from bacterium Serratia proteamaculans (SpChiD) is found to exhibit both hydrolysis and transglycosylation activities. SpChiD belongs to family 18 of glycosyl hydrolases (GH-18). The recombinant SpChiD was crystallized and its three-dimensional structure was determined at 1.49 A resolution. The structure was refined to an R-factor of 16.2%. SpChiD consists of 406 amino acid residues. The polypeptide chain of SpChiD adopts a (beta/alpha)8 triosephosphate isomerase (TIM) barrel structure. SpChiD contains three acidic residues, Asp149, Asp151 and Glu153 as part of its catalytic scheme. While both Asp149 and Glu153 adopt single conformations, Asp151 is observed in two conformations. The substrate binding cleft is partially obstructed by a protruding loop, Asn30 - Asp42 causing a considerable reduction in the number of available subsites in the substrate binding site. The positioning of loop, Asn30 - Asp42 appears to be responsible for the transglycosylation activity. The structure determination indicated the presence of sulfone Met89 (SMet89). The sulfone methionine residue is located on the surface of the protein at a site where extra domain is attached in other chitinases. This is the first structure of a single domain chitinase with hydrolytic and transglycosylation activities. Structure of chitinase D from Serratia proteamaculans reveals the structural basis of its dual action of hydrolysis and transglycosylation.,Madhuprakash J, Singh A, Kumar S, Sinha M, Kaur P, Sharma S, Podile AR, Singh TP Int J Biochem Mol Biol. 2013 Dec 15;4(4):166-78. eCollection 2013. PMID:24380021 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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