4toq | pdb_00004toq

Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity

spinqualitylabelsall models 4toq, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4toq is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, MG Activity: Chitinase, with EC number 3.2.1.14 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Chitinase hydrolyzes the beta-1,4-glycosidic bond in chitin. In higher plants, this enzyme has been regarded as a pathogenesis-related protein. Recently, we identified a class III chitinase, which functions as a calcium storage protein in pomegranate (Punica granatum) seed (PSC, pomegranate seed chitinase). Here, we solved a crystal structure of PSC at 1.6 A resolution. Although its overall structure, including the structure of catalytic site and non-proline cis-peptides, was closely similar to those of other class III chitinases, PSC had some unique structural characteristics. First, there were some metal-binding sites with coordinated water molecules on the surface of PSC. Second, many unconserved aspartate residues were present in the PSC sequence which rendered the surface of PSC negatively charged. This acidic electrostatic property is in contrast to that of hevamine, well-characterized plant class III chitinase, which has rather a positively charged surface. Thus, the crystal structure provides a clue for metal association property of PSC. Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity.,Masuda T, Zhao G, Mikami B Biosci Biotechnol Biochem. 2014 Sep 25:1-6. PMID:25252615 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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