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1LME

Crystal Structure of Peptide Deformylase from Thermotoga maritima

Summary for 1LME
Entry DOI10.2210/pdb1lme/pdb
Related1lm4 1lm6
Descriptorpeptide deformylase (2 entities in total)
Functional Keywordsthermophile, pdf, peptide deformylase, metalloenzyme, deformylation, structural genomics, psi, protein structure initiative, joint center for structural genomics, jcsg, hydrolase
Biological sourceThermotoga maritima
Total number of polymer chains2
Total formula weight41127.54
Authors
Kreusch, A.,Spraggon, G.,Lee, C.C.,Klock, H.,McMullan, D.,Ng, K.,Shin, T.,Vincent, J.,Warner, I.,Ericson, C.,Lesley, S.A.,Joint Center for Structural Genomics (JCSG) (deposition date: 2002-05-01, release date: 2003-06-24, Last modification date: 2023-11-15)
Primary citationKreusch, A.,Spraggon, G.,Lee, C.C.,Klock, H.,McMullan, D.,Ng, K.,Shin, T.,Vincent, J.,Warner, I.,Ericson, C.,Lesley, S.A.
Structure analysis of peptide deformylases from streptococcus pneumoniae,staphylococcus aureus, thermotoga maritima, and pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase
J.MOL.BIOL., 330:309-321, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12823970
DOI: 10.1016/S0022-2836(03)00596-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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数据于2025-08-27公开中

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