2bml | pdb_00002bml

Ofloxacin-like antibiotics inhibit pneumococcal cell wall degrading virulence factors

spinqualitylabelsall models 2bml, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bml is a 2 chain structure with sequence from "diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: P6G, PG4, SO4, TRS, XED Related: 1gvm, 1h8g, 1hcx Activity: N-acetylmuramoyl-L-alanine amidase, with EC number 3.5.1.28 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ALYS_STRPN] Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Autolysin strictly depends on the presence of choline-containing cell walls for activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 produced similar effects on other enzymes with different catalytic activities but that contained a similar choline binding domain; that is, autolysin (LytC) and the phage lytic enzyme (Cpl-1). Finally, we resolved the crystal structure of the complex between the choline binding domain of LytA and ofloxacin at a resolution of 2.6 Angstroms. These data constitute an important launch pad from which effective drugs to combat pneumococcal infections can be developed. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA