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5BWI

Crystallographic structure of a bacterial heparanase

Summary for 5BWI
Entry DOI10.2210/pdb5bwi/pdb
DescriptorGlycoside Hydrolase Family 79, GLYCEROL, ACETATE ION, ... (5 entities in total)
Functional Keywordsglucuronidase, hydrolase
Biological sourceBurkholderia pseudomallei
Total number of polymer chains2
Total formula weight91089.07
Authors
Yu, X.,Blanchard, H. (deposition date: 2015-06-08, release date: 2015-10-28, Last modification date: 2023-09-27)
Primary citationBohlmann, L.,Tredwell, G.D.,Yu, X.,Chang, C.W.,Haselhorst, T.,Winger, M.,Dyason, J.C.,Thomson, R.J.,Tiralongo, J.,Beacham, I.R.,Blanchard, H.,von Itzstein, M.
Functional and structural characterization of a heparanase.
Nat.Chem.Biol., 11:955-957, 2015
Cited by
PubMed 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.
PubMed: 26565989
DOI: 10.1038/nchembio.1956
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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