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 languageEnglish
Pages (from-to)1407-1415
Number of pages9
JournalBiochimie
Volume92
Issue number10
DOIs
Publication statusPublished - 1 Oct 2010

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Crystal structure
Enzymes
Aspartic Acid
Catalytic Domain
Salts
Catalysts
Acids
Proteins

Keywords

  • Acidophilic
  • Crystal structure
  • Family 11 endoxylanase
  • PH adaptation
  • Structure/function relationship

Cite this

@article{7a435143e2764c3cb38c1dfc2eb95918,
title = "Structural insights into the acidophilic pH adaptation of a novel endo-1,4-β-xylanase from Scytalidium acidophilum",
abstract = "In this study, the crystal structure of a novel endo-1,4-β-xylanase from Scytalidium acidophilum, XYL1, was solved at 1.9. {\AA} 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.",
keywords = "Acidophilic, Crystal structure, Family 11 endoxylanase, PH adaptation, Structure/function relationship",
author = "Catherine Michaux and Jenny Pouyez and Aur{\'e}lie Mayard and Pierre Vandurm and Isabelle Housen and Johan Wouters",
year = "2010",
month = "10",
day = "1",
doi = "10.1016/j.biochi.2010.07.003",
language = "English",
volume = "92",
pages = "1407--1415",
journal = "Biochimie",
issn = "0300-9084",
publisher = "Elsevier",
number = "10",

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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

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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 -