3WSU
Crystal structure of beta-mannanase from Streptomyces thermolilacinus
Summary for 3WSU
| Entry DOI | 10.2210/pdb3wsu/pdb |
| Related | 4Y7E |
| Descriptor | Beta-mannanase, SODIUM ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | mannanase, glycoside hydrolase family 5, actinomycete, hydrolase |
| Biological source | Streptomyces thermolilacinus |
| Total number of polymer chains | 2 |
| Total formula weight | 75435.40 |
| Authors | Kumagai, Y.,Yamashita, K.,Okuyama, M.,Hatanaka, T.,Yao, M.,Kimura, A. (deposition date: 2014-03-26, release date: 2015-05-20, Last modification date: 2023-11-08) |
| Primary citation | Kumagai, Y.,Yamashita, K.,Tagami, T.,Uraji, M.,Wan, K.,Okuyama, M.,Yao, M.,Kimura, A.,Hatanaka, T. The loop structure of Actinomycete glycoside hydrolase family 5 mannanases governs substrate recognition Febs J., 282:4001-4014, 2015 Cited by PubMed Abstract: Endo-β-1,4-mannanases from Streptomyces thermolilacinus (StMan) and Thermobifida fusca (TfMan) demonstrated different substrate specificities. StMan hydrolyzed galactosylmannooligosaccharide (GGM5; 6(III) ,6(IV) -α-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 Å, 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. PubMed: 26257335DOI: 10.1111/febs.13401 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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