| Literature DB >> 26565989 |
Lisa Bohlmann1, Gregory D Tredwell1, Xing Yu1, Chih-Wei Chang1, Thomas Haselhorst1, Moritz Winger1, Jeffrey C Dyason1, Robin J Thomson1, Joe Tiralongo1, Ifor R Beacham1, Helen Blanchard1, Mark von Itzstein1.
Abstract
We report the structural and functional characterization of a novel heparanase (BpHep) from the invasive pathogenic bacterium Burkholderia pseudomallei (Bp), showing ∼24% sequence identity with human heparanase (hHep). Site-directed mutagenesis studies confirmed the active site resi-dues essential for activity, and we found that BpHep has specificity for heparan sulfate. Finally, we describe the first heparanase X-ray crystal structure, which provides new insight into both substrate recognition and inhibitor design.Entities:
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Year: 2015 PMID: 26565989 DOI: 10.1038/nchembio.1956
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040