1NQ6
Crystal Structure of the catalytic domain of xylanase A from Streptomyces halstedii JM8
Summary for 1NQ6
| Entry DOI | 10.2210/pdb1nq6/pdb |
| Descriptor | Xys1, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | glycoside hydrolase family 10, xylanase, xylan degradation, hydrolase |
| Biological source | Streptomyces halstedii |
| Total number of polymer chains | 1 |
| Total formula weight | 32638.38 |
| Authors | Canals, A.,Vega, M.C.,Gomis-Ruth, F.X.,Santamaria, R.I.,Coll, M. (deposition date: 2003-01-21, release date: 2004-01-21, Last modification date: 2024-11-13) |
| Primary citation | Canals, A.,Vega, M.C.,Gomis-Ruth, F.X.,Diaz, M.,Santamaria R, R.I.,Coll, M. Structure of xylanase Xys1delta from Streptomyces halstedii. Acta Crystallogr.,Sect.D, 59:1447-1453, 2003 Cited by PubMed Abstract: Xylanases hydrolyze the beta-1,4-linked xylose backbone of xylans. They are of increasing interest in the paper and food industries for their pre-bleaching and bio-pulping applications. Such industries demand new xylanases to cover a wider range of cleavage specificity, activity and stability. The catalytic domain of xylanase Xys1 from Streptomyces halstedii JM8 was expressed, purified and crystallized and native data were collected to 1.78 A resolution with an R(merge) of 4.4%. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.05, b = 79.60, c = 87.80 A. The structure was solved by the molecular-replacement method using the structure of the homologue Xyl10A from Streptomyces lividans. In a similar manner to other members of its family, Xys1 folds to form a standard (beta/alpha)(8) barrel with the two catalytic functions, the acid/base and the nucleophile, at its C-terminal side. The overall structure is described and compared with those of related xylanases. PubMed: 12876348DOI: 10.1107/S0907444903012629 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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