3M4F
Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum
Summary for 3M4F
| Entry DOI | 10.2210/pdb3m4f/pdb |
| Descriptor | Endo-1,4-beta-xylanase, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID (3 entities in total) |
| Functional Keywords | family 11 endoxylanase, acidophilic adaptation, structure/function relationship, glycosidase, hydrolase, xylan degradation |
| Biological source | Scytalidium acidophilum |
| Total number of polymer chains | 4 |
| Total formula weight | 88371.76 |
| Authors | Michaux, C.,Wouters, J. (deposition date: 2010-03-11, release date: 2010-07-28, Last modification date: 2024-10-30) |
| Primary citation | Michaux, C.,Pouyez, J.,Mayard, A.,Vandurm, P.,Housen, I.,Wouters, J. Structural insights into the acidophilic pH adaptation of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum Biochimie, 92:1407-1415, 2010 Cited by PubMed Abstract: In this study, the crystal structure of a novel endo-1,4-β-xylanase from Scytalidium acidophilum, XYL1, was solved at 1.9Å resolution. This is one of the few solved crystal structures of acidophilic proteins. The enzyme has the overall fold typical to family 11 xylanases. Comparison of this structure with other homologous acidophilic, neutrophilic and alkalophilic xylanases provides additional insights into the general features involved in low pH adaptation (stability and activity). Several sequence and structure modifications appeared to be responsible for the acidophilic characteristic: (a) the presence of an aspartic acid H bonded to the acid/base catalyst (b) the nature of specifically conserved residues in the active site (c) the negative potential at the surface (d) the decreased number of salt bridges and H bonds in comparison with highly alkaline enzymes. PubMed: 20621155DOI: 10.1016/j.biochi.2010.07.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.89 Å) |
Structure validation
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