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Forest Products Laboratory
One Gifford Pinchot Drive
Madison, WI 53726-2398
Phone: (608) 231-9200
Fax: (608) 231-9592
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Researchers Determine the Structure of Bacterial Protein Involved in Biomass Conversion

Image 1: A picture of PbXynA1 (an xylanases enzyme) with the a xylooligosaccharide (sugar polymer) bound into the active site. Image 2: A close up revealing a large pocket not previously observed in other xylanases (enzymes) of this family. Franz St John, USDA Forest Service
Image 1: A picture of PbXynA1 (an xylanases enzyme) with the a xylooligosaccharide (sugar polymer) bound into the active site. Image 2: A close up revealing a large pocket not previously observed in other xylanases (enzymes) of this family. Franz St John, USDA Forest Service
Snapshot: Researchers structurally characterized a bacterial protein involved in biomass degradation. The knowledge obtained from this novel protein suggest that it may function better than comparable enzymes in targeting complex lignocellulosic biomass.
Summary:

Xylanases are important enzymes involved in the degradation of the second most abundant sugar polymer in woody biomass. This sugar can constitute up to 25 percent of the total mass of trees. The bacterial xylanase XynA1 is a large, cell-surface-anchored enzyme consisting of several separate protein domains. Together, these domains create a biological system which binds to soluble xylans, degrades the polysaccharide chains and delivers the small sugars near to the cell surface for efficient assimilation for bioconversion to value-added products or fuels. In this work, Forest Service researchers, together with collaborators from the University of Maryland, Baltimore and the University of Florida have determined the three-dimentional protein structure of the xylanase catalytic domain. This structure has revealed numerous features which are thought to provide enhanced functionality relative to other, similar enzymes. The region of this enzyme that binds to and cleaves xylan contains a large opening which may be used to accommodate chemical appendages along the xylan chain. This observation may indicate a more efficient interaction with chemically complex xylan substrates relative to similar xylanase enzymes. These findings are important as they contribute to the identification new enzymes which may be applicable to microbial bioconversion of low-value woody biomass substrates.
Princpal Investigator(s):
 St. Johns, Franz


Research Location:
  • Forest Products Laboratory, Madison, WI
  • University of Maryland, Baltimore, MD


External Partners:
  • University of Florida
  • University of Maryland

Fiscal Year: 2013
Highlight ID: 452
 
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