Structural insights into the acidophilic pH adaptation of a novel endo-1,4-β-xylanase from Scytalidium acidophilum
| Autor: | Catherine Michaux, Jenny Pouyez, Isabelle Housen, Johan Wouters, Pierre Vandurm, Aurélie Mayard |
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| Rok vydání: | 2010 |
| Předmět: |
Protein Conformation
PH adaptation Static Electricity Crystal structure Crystallography X-Ray Biochemistry Fungal Proteins Protein structure Ascomycota Catalytic Domain Aspartic acid Hydrolase Static electricity Structure/function relationship chemistry.chemical_classification Endo-1 4-beta Xylanases biology Hydrogen bond Active site Hydrogen Bonding General Medicine Family 11 endoxylanase Hydrogen-Ion Concentration Acidophilic Adaptation Physiological Enzyme chemistry biology.protein |
| Zdroj: | Biochimie. 92:1407-1415 |
| ISSN: | 0300-9084 |
| DOI: | 10.1016/j.biochi.2010.07.003 |
| Popis: | In this study, the crystal structure of a novel endo-1,4-β-xylanase from Scytalidium acidophilum, XYL1, was solved at 1.9. Å 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. |
| Databáze: | OpenAIRE |
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