1lm6
From Proteopedia
(New page: 200px<br /><applet load="1lm6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lm6, resolution 1.75Å" /> '''Crystal Structure of...) |
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| - | [[Image:1lm6.gif|left|200px]]<br /><applet load="1lm6" size=" | + | [[Image:1lm6.gif|left|200px]]<br /><applet load="1lm6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lm6, resolution 1.75Å" /> | caption="1lm6, resolution 1.75Å" /> | ||
'''Crystal Structure of Peptide Deformylase from Streptococcus pneumoniae'''<br /> | '''Crystal Structure of Peptide Deformylase from Streptococcus pneumoniae'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Peptide deformylase (PDF) has received considerable attention during the | + | 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== | ==About this Structure== | ||
| - | 1LM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with FE and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1LM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LM6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Klock, H.]] | [[Category: Klock, H.]] | ||
[[Category: Kreusch, A.]] | [[Category: Kreusch, A.]] | ||
| - | [[Category: Lee, C | + | [[Category: Lee, C C.]] |
| - | [[Category: Lesley, S | + | [[Category: Lesley, S A.]] |
[[Category: McMullan, D.]] | [[Category: McMullan, D.]] | ||
[[Category: Ng, K.]] | [[Category: Ng, K.]] | ||
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[[Category: peptide deformylase]] | [[Category: peptide deformylase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:13 2008'' |
Revision as of 11:46, 21 February 2008
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Crystal Structure of Peptide Deformylase from Streptococcus pneumoniae
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
1LM6 is a Single protein structure of sequence from Streptococcus pneumoniae with and as ligands. Active as Peptide deformylase, with EC number 3.5.1.88 Full crystallographic information is available from 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:12823970
Page seeded by OCA on Thu Feb 21 13:46:13 2008
Categories: Peptide deformylase | Single protein | Streptococcus pneumoniae | Ericson, C. | Klock, H. | Kreusch, A. | Lee, C C. | Lesley, S A. | McMullan, D. | Ng, K. | Shin, T. | Spraggon, G. | Vincent, J. | Warner, I. | FE | GOL | Metalloenzyme | Pdf
