3wsu

Crystal structure of beta-mannanase from Streptomyces thermolilacinus

spinqualitylabelsall models 3wsu, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wsu is a 2 chain structure with sequence from Streptomyces thermolilacinus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: GOL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F5HR99_9ACTN Publication Abstract from PubMed Endo-beta-1,4-mannanases from Streptomyces thermolilacinus (StMan) and Thermobifida fusca (TfMan) demonstrated different substrate specificities. StMan hydrolyzed galactosylmannooligosaccharide (GGM5; 6III ,6IV -alpha-d-galactosyl mannopentaose) to GGM3 and M2, whereas TfMan hydrolyzed GGM5 to GGM4 and M1. To determine the region involved in the substrate specificity, we constructed chimeric enzymes of StMan and TfMan and evaluated their substrate specificities. Moreover, the crystal structure of the catalytic domain of StMan (StMandC) and the complex structure of the inactive mutant StE273AdC with M6 were solved at resolutions of 1.60 and 1.50 A, respectively. Structural comparisons of StMandC and the catalytic domain of TfMan lead to the identification of a subsite around -1 in StMandC that could accommodate a galactose branch. These findings demonstrate that the two loops (loop7 and loop8) are responsible for substrate recognition in GH5 actinomycete mannanases. In particular, Trp281 in loop7 of StMan, which is located in a narrow and deep cleft, plays an important role in its affinity toward linear substrates. Asp310 in loop8 of StMan specifically bound to the galactosyl unit in the -1 subsite. The loop structure of Actinomycete glycoside hydrolase family 5 mannanases governs substrate recognition.,Kumagai Y, Yamashita K, Tagami T, Uraji M, Wan K, Okuyama M, Yao M, Kimura A, Hatanaka T FEBS J. 2015 Aug 9. doi: 10.1111/febs.13401. PMID:26257335 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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