Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 299, Issue 4, Pages 885-895Publisher
ACADEMIC PRESS LTD
DOI: 10.1006/jmbi.2000.3817
Keywords
hyaluronic acid; hyaluronate lyase; enzyme-product complex; hyaluronan-degradation mechanism; X-ray structure
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Funding
- NIAID NIH HHS [R01 AI 44079] Funding Source: Medline
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Hyaluronic acid (HA) is an important constituent of the extracellular matrix; its bacterial degradation has been postulated to contribute to the spread of certain streptococci through tissue. Pneumococci and other streptococci produce hyaluronate lyase, an enzyme which depolymerizes HA, thus hyaluronate lyase might contribute directly to bacterial invasion. Although two different mechanisms for lyase action have been proposed, there was no crystallographic evidence to support those mechanisms. Here, we report the high-resolution crystal structure of Streptococcus pneumoniae hyaluronate lyase in the presence of HA disaccharide product, which ultimately provides the first crystallographic evidence for the binding of HA to hyaluronate lyase. This structural complex revealed a key interaction between the Streptococcus peneumoniae hyaluronate lyase protein and the product, and supports our previously proposed novel catalytic mechanism for HA degradation based on the native Streptococcus peneumoniae hyaluronate lyase structure. The information provided by this complex structure will likely be useful in the development of antimicrobial pharmaceutical agents. (C) 2000 Academic Press.
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