3ur7 | pdb_00003ur7

Higher-density crystal structure of potato endo-1,3-beta-glucanase

spinqualitylabelsall models 3ur7, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ur7 is a 2 chain structure with sequence from Potato. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NA Related: 1ghs, 2cyg, 3em5, 3f55, 3ur8 Gene: gluB20-2 (Potato) Activity: Glucan endo-1,3-beta-D-glucosidase, with EC number 3.2.1.39 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Endo-1,3-beta-glucanases are widely distributed among bacteria, fungi and higher plants. They are responsible for hydrolysis of the glycosidic bond in specific polysaccharides with tracts of unsubstituted beta-1,3-linked glucosyl residues. The plant enzymes belong to glycoside hydrolase family 17 (GH17) and are also members of class 2 of pathogenesis-related (PR) proteins. X-ray diffraction data were collected to 1.40 and 1.26 A resolution from two crystals of endo-1,3-beta-glucanase from Solanum tuberosum (potato, cultivar Desiree) which, despite having a similar packing framework, represented two separate crystal forms. In particular, they differed in the Matthews coefficient and are consequently referred to as higher density (HD; 1.40 A resolution) and lower density (LD; 1.26 A resolution) forms. The general fold of the protein resembles that of other known plant endo-1,3-beta-glucanases and is defined by a (beta/alpha)(8)-barrel with an additional subdomain built around the C-terminal half of the barrel. The structures revealed high flexibility of the subdomain, which forms part of the catalytic cleft. Comparison with structures of other GH17 endo-1,3-beta-glucanases revealed differences in the arrangement of the secondary-structure elements in this region, which can be correlated with sequence variability and may suggest distinct substrate-binding patterns. The crystal structures revealed an unusual packing mode, clearly visible in the LD structure, caused by the presence of the C-terminal His(6) tag, which extends from the compact fold of the enzyme molecule and docks in the catalytic cleft of a neighbouring molecule. In this way, an infinite chain of His-tag-linked protein molecules is formed along the c direction. Two high-resolution structures of potato endo-1,3-beta-glucanase reveal subdomain flexibility with implications for substrate binding.,Wojtkowiak A, Witek K, Hennig J, Jaskolski M Acta Crystallogr D Biol Crystallogr. 2012 Jun;68(Pt 6):713-23. doi:, 10.1107/S090744491200995X. Epub 2012 May 17. PMID:22683794 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase

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