Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 1407-1415 |
| Number of pages | 9 |
| Journal | Biochimie |
| Volume | 92 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - 1 Oct 2010 |
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Keywords
- Acidophilic
- Crystal structure
- Family 11 endoxylanase
- PH adaptation
- Structure/function relationship
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Structural insights into the acidophilic pH adaptation of a novel endo-1,4-β-xylanase from Scytalidium acidophilum. / Michaux, Catherine; Pouyez, Jenny; Mayard, Aurélie; Vandurm, Pierre; Housen, Isabelle; Wouters, Johan.
In: Biochimie, Vol. 92, No. 10, 01.10.2010, p. 1407-1415.Research output: Contribution to journal › Article
TY - JOUR
T1 - Structural insights into the acidophilic pH adaptation of a novel endo-1,4-β-xylanase from Scytalidium acidophilum
AU - Michaux, Catherine
AU - Pouyez, Jenny
AU - Mayard, Aurélie
AU - Vandurm, Pierre
AU - Housen, Isabelle
AU - Wouters, Johan
PY - 2010/10/1
Y1 - 2010/10/1
N2 - 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.
AB - 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.
KW - Acidophilic
KW - Crystal structure
KW - Family 11 endoxylanase
KW - PH adaptation
KW - Structure/function relationship
UR - http://www.scopus.com/inward/record.url?scp=77957153923&partnerID=8YFLogxK
U2 - 10.1016/j.biochi.2010.07.003
DO - 10.1016/j.biochi.2010.07.003
M3 - Article
C2 - 20621155
AN - SCOPUS:77957153923
VL - 92
SP - 1407
EP - 1415
JO - Biochimie
JF - Biochimie
SN - 0300-9084
IS - 10
ER -