Novel structural features of xylanase A1 from Paenibacillus sp. JDR-2

Franz St. John; James F. Preston; Edwin Pozharski

doi:10.1016/j.jsb.2012.09.007

Treesearch

Novel structural features of xylanase A1 from Paenibacillus sp. JDR-2

Formally Refereed

Authors:

Franz St. John, James F. Preston, Edwin Pozharski

Year:

2012

Type:

Scientific Journal

Station:

Forest Products Laboratory

DOI:

https://doi.org/10.1016/j.jsb.2012.09.007

Source:

Journal of Structural Biology 180, 2012; pp. 303–311.

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Abstract

The Gram-positive bacterium Paenibacillus sp. JDR-2 (PbJDR2) has been shown to have novel properties in the utilization of the abundant but chemically complex hemicellulosic sugar glucuronoxylan. Xylanase A1 of PbJDR2 (PbXynA1) has been implicated in an efficient process in which extracellular depolymerization of this polysaccharide is coupled to assimilation and intracellular metabolism. PbXynA1is a 154 kDa cell wall anchored multimodular glycosyl hydrolase family 10 (GH10) xylanase. In this work, the 38 kDa catalytic module of PbXynA1 has been structurally characterized revealing several new features not previously observed in structures of GH10 xylanases. These features are thought to facilitate hydrolysis of highly substituted, chemically complex xylans that may be the form found in close proximity to the cell wall of PbJDR2, an organism shown to have a preference for growth on polymeric glucuronoxylan.

Keywords

Paenibacillus, molar xylanase, GH10, Glycosyl hydrolase family 10, GH 10 structure

Citation

St. John, Franz J.; Preston, James F.; Pozharski, Edwin. 2012. Novel structural features of xylanase A1 from Paenibacillus sp. JDR-2. Journal of Structural Biology. 180: 303-311.