3M4F: Structural Insights Into The Acidophilic Ph Adaptation Of A Novel Endo-1,4-Beta-Xylanase From Scytalidium Acidophilum

In this study, the crystal structure of a novel endo-1,4-beta-xylanase from Scytalidium acidophilum, XYL1, was solved at 1.9A 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 alkalineenzymes.
PDB ID: 3M4FDownload
MMDB ID: 83625
PDB Deposition Date: 2010/3/11
Updated in MMDB: 2010/10
Experimental Method:
x-ray diffraction
Resolution: 1.89  Å
Source Organism:
Similar Structures:
Biological Unit for 3M4F: monomeric; determined by author and by software (PISA)
Molecular Components in 3M4F
Label Count Molecule
Protein (1 molecule)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

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