2bml
From Proteopedia
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|PDB= 2bml |SIZE=350|CAPTION= <scene name='initialview01'>2bml</scene>, resolution 2.60Å | |PDB= 2bml |SIZE=350|CAPTION= <scene name='initialview01'>2bml</scene>, resolution 2.60Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=XED:DEXTROFLOXACINE'>XED</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/N-acetylmuramoyl-L-alanine_amidase N-acetylmuramoyl-L-alanine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.28 3.5.1.28] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylmuramoyl-L-alanine_amidase N-acetylmuramoyl-L-alanine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.28 3.5.1.28] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bml OCA], [http://www.ebi.ac.uk/pdbsum/2bml PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bml RCSB]</span> | ||
}} | }} | ||
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[[Category: Pascual-Teresa, B D.]] | [[Category: Pascual-Teresa, B D.]] | ||
[[Category: Romero, A.]] | [[Category: Romero, A.]] | ||
| - | [[Category: P6G]] | ||
| - | [[Category: PG4]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: TRS]] | ||
| - | [[Category: XED]] | ||
[[Category: cell wall attachment]] | [[Category: cell wall attachment]] | ||
[[Category: choline-binding domain]] | [[Category: choline-binding domain]] | ||
[[Category: ofloxacin-like antibiotic]] | [[Category: ofloxacin-like antibiotic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:08:39 2008'' |
Revision as of 23:08, 30 March 2008
| |||||||
| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , | ||||||
| Activity: | N-acetylmuramoyl-L-alanine amidase, with EC number 3.5.1.28 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 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.
About this Structure
2BML is a Single protein structure of sequence from Streptococcus pneumoniae. 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
Page seeded by OCA on Mon Mar 31 02:08:39 2008
