2brp
From Proteopedia
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CRYSTAL STRUCTURE OF S.PNEUMONIAE HYALURONATE LYASE IN COMPLEX WITH W249B
Overview
The bacterial hyaluronan lyases (Hyals) that degrade hyaluronan, an, important component of the extracellular matrix, are involved in microbial, spread. Inhibitors of these enzymes are essential in investigation of the, role of hyaluronan and Hyal in bacterial infections and constitute a new, class of antibiotics against Hyal-producing bacteria. Recently, we, identified 1,3-diacetylbenzimidazole-2-thione and related molecules as, inhibitors of streptococcal Hyal. One of such compounds, 1-decyl-2-(4-sulfamoyloxyphenyl)-1-indol-6-yl sulfamate, was, co-crystallized in a complex with Streptococcus pneumoniae Hyal and its, structure elucidated. The resultant X-ray structure demonstrates that this, inhibitor fits in the enzymatic active site via interactions resembling, the binding mode of the ... [(full description)]
About this Structure
2BRP is a [Single protein] structure of sequence from [Streptococcus pneumoniae] with XLS, SO4 and SIE as [ligands]. Active as [Hyaluronate lyase], with EC number [4.2.2.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Design of new benzoxazole-2-thione-derived inhibitors of Streptococcus pneumoniae hyaluronan lyase: structure of a complex with a 2-phenylindole., Rigden DJ, Botzki A, Nukui M, Mewbourne RB, Lamani E, Braun S, von Angerer E, Bernhardt G, Dove S, Buschauer A, Jedrzejas MJ, Glycobiology. 2006 Aug;16(8):757-65. Epub 2006 Apr 25. PMID:16638841
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