24tf

Crystal structure of GH30 endo-beta-1,6-galactanase from Streptomyces avermitilis soaked with Gal-beta1,6-Gal-beta1,6-Gal.

spinqualitylabelsall models 24tf, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 24tf is a 1 chain structure with sequence from Streptomyces avermitilis MA-4680 = NBRC 14893. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: GAL, GOL, MES, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q82CY3_STRAW Publication Abstract from PubMed Endo-beta-1,6-galactanases hydrolyze beta-1,6-linked galactosyl linkages in galactans, yielding beta-1,6-linked galacto-oligosaccharides, predominantly galactobiose. Here, we report to our knowledge the first crystal structure of an endo-beta-1,6-galactanase, together with its beta-1,6-galactobiose-bound complex, revealing the structural basis for substrate recognition by this enzyme. Endo-beta-1,6-galactanase from Streptomyces avermitilis (Sa16Gal30A) is a member of glycoside hydrolase family 30 (GH30) subfamily 5. Sa16Gal30A consists of two structural domains: a catalytic (beta/alpha)(8)-barrel domain and an appended beta-sandwich domain. The beta-1,6-galactobiose complex structure revealed two beta-1,6-galactobiose molecules bound within the catalytic domain: one at the catalytic site and another at the distinct surface site distal to the catalytic center. This structure represents the first reported structure of a GH30 subfamily 5 enzyme and provides structural insights into the molecular basis of beta-1,6-galactan recognition within the catalytic cleft. Sa16Gal30A possesses three extended regions, loops 2, 4 and 8, in the catalytic domain compared with enzymes from other GH30 subfamilies, and these loops appear to modulate substrate specificity towards beta-1,6-galactan by shaping the architecture of the catalytic cleft. In addition, a secondary beta-1,6-galactan-binding site was identified at a distal location, which may function as a distal subsite, thereby facilitating the efficient hydrolysis of long beta-1,6-galactan chains. Crystal structure of endo-beta-1,6-galactanase from Streptomyces avermitilis.,Fujimoto Z, Kishine N, Kotake T, Kaneko S Acta Crystallogr D Struct Biol. 2026 Aug 1;82(Pt 8):962-971. doi: , 10.1107/S2059798326006133. Epub 2026 Jul 21. PMID:42478457 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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