1FHL
CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 293K
Summary for 1FHL
| Entry DOI | 10.2210/pdb1fhl/pdb |
| Related | 1FOB |
| Descriptor | BETA-1,4-GALACTANASE (2 entities in total) |
| Functional Keywords | b/a barrel, glycosyl hydrolase, family 53, clan gh-a, hydrolase |
| Biological source | Aspergillus aculeatus |
| Total number of polymer chains | 1 |
| Total formula weight | 36775.44 |
| Authors | Ryttersgaard, C.,Larsen, S. (deposition date: 2000-08-02, release date: 2003-06-03, Last modification date: 2024-11-06) |
| Primary citation | Ryttersgaard, C.,Leggio, L.L.,Coutinho, P.M.,Henrissat, B.,Larsen, S. Aspergillus aculeatus beta-1,4-Galactanase: Substrate Recognition and Relations to Other Glycoside Hydrolases in Clan GH-A Biochemistry, 41:15135-15143, 2002 Cited by PubMed Abstract: The three-dimensional structure of Aspergillus aculeatus beta-1,4-galactanase (AAGAL), an enzyme involved in pectin degradation, has been determined by multiple isomorphous replacement to 2.3 and 1.8 A resolution at 293 and 100 K, respectively. It represents the first known structure for a polysaccharidase with this specificity and for a member of glycoside hydrolase family 53 (GH-53). The enzyme folds into a (beta/alpha)(8) barrel with the active site cleft located at the C-terminal side of the barrel consistent with the classification of GH-53 in clan GH-A, a superfamily of enzymes with common fold and catalytic machinery but diverse specificities. Putative substrate-enzyme interactions were elucidated by modeling of beta-1,4-linked galactobioses into the possible substrate binding subsites. The structure and modeling studies identified five potential subsites for the binding of galactans, of which one is a pocket suited for accommodating the arabinan side chain in arabinogalactan, one of the natural substrates. A comparison with the substrate binding grooves of other Clan GH-A enzymes suggests that shape complementarity is crucial in determining the specificity of polysaccharidases. PubMed: 12484750DOI: 10.1021/bi026238c PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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