1lqw
From Proteopedia
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|PDB= 1lqw |SIZE=350|CAPTION= <scene name='initialview01'>1lqw</scene>, resolution 1.87Å | |PDB= 1lqw |SIZE=350|CAPTION= <scene name='initialview01'>1lqw</scene>, resolution 1.87Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1lqy|1LQY]], [[1lru|1LRU]], [[1lry|1LRY]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqw OCA], [http://www.ebi.ac.uk/pdbsum/1lqw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lqw RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Mikol, V.]] | [[Category: Mikol, V.]] | ||
| - | [[Category: ZN]] | ||
[[Category: pdf]] | [[Category: pdf]] | ||
[[Category: peptide deformylase]] | [[Category: peptide deformylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:06:14 2008'' |
Revision as of 19:06, 30 March 2008
| |||||||
| , resolution 1.87Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Peptide deformylase, with EC number 3.5.1.88 | ||||||
| Related: | 1LQY, 1LRU, 1LRY
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of S.aureus Peptide Deformylase
Overview
Bacterial peptide deformylase (PDF) belongs to a sub-family of metalloproteases that catalyse the removal of the N-terminal formyl group from newly synthesised proteins. PDF is essential in prokaryotes and conserved throughout the eubacteria. It is therefore considered an attractive target for developing new antibacterial agents. Here, we report the crystal structures of four bacterial deformylases, free or bound to the naturally occurring antibiotic actinonin, including two from the major bacterial pathogens Pseudomonas aeruginosa and Staphylococcus aureus. The overall tertiary structure is essentially conserved but shows significant differences, namely at the C terminus, which are directly related to the deformylase type (i.e. I or II) they belong to. The geometry around the catalytic metal ion exhibits a high level of similarity within the different enzymes, as does the binding mode of actinonin to the various deformylases. However, some significant structural differences are found in the vicinity of the active site, highlighting the structural and molecular requirements for the design of a deformylase inhibitor active against a broad spectrum of bacterial strains.
About this Structure
1LQW is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents., Guilloteau JP, Mathieu M, Giglione C, Blanc V, Dupuy A, Chevrier M, Gil P, Famechon A, Meinnel T, Mikol V, J Mol Biol. 2002 Jul 26;320(5):951-62. PMID:12126617
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