2hvm | pdb_00002hvm

HEVAMINE A AT 1.8 ANGSTROM RESOLUTION

spinqualitylabelsall models 2hvm, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hvm is a 1 chain structure with sequence from Hevea brasiliensis. This structure supersedes the now removed PDB entry 1hvm. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CHLY_HEVBR] Bifunctional enzyme with lysozyme / chitinase activity. May have a role in plugging the latex vessel and cessation of latex flow. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The three-dimensional structure of hevamine, a plant enzyme with chitinase and lysozyme activity, has been refined at 1.8 A resolution to an R-factor of 14.9% and a free R-factor of 19.6%. The final model consists of all 273 amino acid residues and 206 ordered water molecules. Two non-proline cis-peptides were identified, involving Phe32 and Trp255, both of which are implicated in substrate binding. Other glycosyl hydrolase family 18 proteins with known three-dimensional structure are bacterial chitinase A, endo-beta-N-acetylglucosaminidase F1, endo-beta-N-acetylglucosaminidase H, and the two plant proteins concanavalin B and narbonin, which have no known enzymatic activity. All these structures contain a (beta alpha)8 barrel fold, with the two family 18 consensus regions roughly corresponding to the third and fourth barrel strands. This confirms the grouping of these proteins into family 18, which was only based on weak and local sequence similarity. The substrate specificity of the enzymes is determined by the loops following the barrel strands that form the substrate binding site. All enzymes have an aspartic acid and a glutamic acid residue in positions identical with Asp 125 and the catalytic Glu127 of hevamine. The lack of chitinase activity of concanavalin B and narbonin can be explained by the absence of one of these carboxylate groups, and by differences in the loops that form the substrate-binding cleft in hevamine. The 1.8 A resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18.,Terwisscha van Scheltinga AC, Hennig M, Dijkstra BW J Mol Biol. 1996 Sep 20;262(2):243-57. PMID:8831791 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chitinase

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