1lm4: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1lm4 |SIZE=350|CAPTION= <scene name='initialview01'>1lm4</scene>, resolution 1.45Å | |PDB= 1lm4 |SIZE=350|CAPTION= <scene name='initialview01'>1lm4</scene>, resolution 1.45Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> | |LIGAND= <scene name='pdbligand=CSW:CYSTEINE-S-DIOXIDE'>CSW</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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= pdf1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | |GENE= pdf1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1lm6|1LM6]], [[1lme|1LME]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lm4 OCA], [http://www.ebi.ac.uk/pdbsum/1lm4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lm4 RCSB]</span> | |||
}} | }} | ||
| Line 34: | Line 37: | ||
[[Category: Vincent, J.]] | [[Category: Vincent, J.]] | ||
[[Category: Warner, I.]] | [[Category: Warner, I.]] | ||
[[Category: metalloenzyme]] | [[Category: metalloenzyme]] | ||
[[Category: pdf]] | [[Category: pdf]] | ||
[[Category: staphylococcus aureus]] | [[Category: staphylococcus aureus]] | ||
''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 22:04:31 2008'' | ||
Revision as of 22:04, 30 March 2008
| |||||||
| , resolution 1.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | pdf1 (Staphylococcus aureus) | ||||||
| Activity: | Peptide deformylase, with EC number 3.5.1.88 | ||||||
| Related: | 1LM6, 1LME
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Peptide Deformylase from Staphylococcus aureus at 1.45 A
OverviewOverview
Peptide deformylase (PDF) has received considerable attention during the last few years as a potential target for a new type of antibiotics. It is an essential enzyme in eubacteria for the removal of the formyl group from the N terminus of the nascent polypeptide chain. We have solved the X-ray structures of four members of this enzyme family, two from the Gram-positive pathogens Streptococcus pneumoniae and Staphylococcus aureus, and two from the Gram-negative bacteria Thermotoga maritima and Pseudomonas aeruginosa. Combined with the known structures from the Escherichia coli enzyme and the recently solved structure of the eukaryotic deformylase from Plasmodium falciparum, a complete picture of the peptide deformylase structure and function relationship is emerging. This understanding could help guide a more rational design of inhibitors. A structure-based comparison between PDFs reveals some conserved differences between type I and type II enzymes. Moreover, our structures provide insights into the known instability of PDF caused by oxidation of the metal-ligating cysteine residue.
About this StructureAbout this Structure
1LM4 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
Structure analysis of peptide deformylases from Streptococcus pneumoniae, Staphylococcus aureus, Thermotoga maritima and Pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase., Kreusch A, Spraggon G, Lee CC, Klock H, McMullan D, Ng K, Shin T, Vincent J, Warner I, Ericson C, Lesley SA, J Mol Biol. 2003 Jul 4;330(2):309-21. PMID:12823970
Page seeded by OCA on Sun Mar 30 22:04:31 2008