2bml
From Proteopedia
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OFLOXACIN-LIKE ANTIBIOTICS INHIBIT PNEUMOCOCCAL CELL WALL DEGRADING VIRULENCE FACTORS
Overview
The search for new drugs against Streptococcus pneumoniae (pneumococcus), is driven by the 1.5 million deaths it causes annually. Choline-binding, proteins attach to the pneumococcal cell wall through domains that, recognize choline moieties, and their involvement in pneumococcal, virulence makes them potential targets for drug development. We have, defined chemical criteria involved in the docking of small molecules from, a three-dimensional structural library to the major pneumococcal autolysin, (LytA) choline binding domain. These criteria were used to identify, compounds that could interfere with the attachment of this protein to the, cell wall, and several quinolones that fit this framework were found to, inhibit the cell wall-degrading activity of LytA. Furthermore, these, compounds ... [(full description)]
About this Structure
2BML is a [Single protein] structure of sequence from [Streptococcus pneumoniae] with SO4, TRS, P6G, XED and PG4 as [ligands]. Active as [[1]], with EC number [3.5.1.28]. Full crystallographic information is available from [OCA].
Reference
Ofloxacin-like antibiotics inhibit pneumococcal cell wall-degrading virulence factors., Fernandez-Tornero C, Garcia E, de Pascual-Teresa B, Lopez R, Gimenez-Gallego G, Romero A, J Biol Chem. 2005 May 20;280(20):19948-57. Epub 2005 Mar 15. PMID:15769740
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