View source for 1lm4

[[Image:1lm4.gif|left|200px]]

 {{Structure
|PDB= 1lm4 |SIZE=350|CAPTION= <scene name='initialview01'>1lm4</scene>, resolution 1.45&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <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] 
|GENE= pdf1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
}}

'''Structure of Peptide Deformylase from Staphylococcus aureus at 1.45 A'''


==Overview==
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 Structure==
1LM4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LM4 OCA]. 

==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12823970 12823970]
[[Category: Peptide deformylase]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Ericson, C.]]
[[Category: Klock, H.]]
[[Category: Kreusch, A.]]
[[Category: Lee, C C.]]
[[Category: Lesley, S A.]]
[[Category: McMullan, D.]]
[[Category: Ng, K.]]
[[Category: Shin, T.]]
[[Category: Spraggon, G.]]
[[Category: Vincent, J.]]
[[Category: Warner, I.]]
[[Category: FE]]
[[Category: GOL]]
[[Category: metalloenzyme]]
[[Category: pdf]]
[[Category: staphylococcus aureus]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:32:26 2008''