| Title | 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 | | Site | JCSG | | PDB Id | | Target Id | 283518 | | Molecular Characteristics | | Source | Thermotoga maritima msb8 | | Alias Ids | TPS1309,TM1661 | Molecular Weight | 19023.15 Da. | | Residues | 164 | Isoelectric Point | 7.82 | | Sequence | myrirvfgdpvlrkrakpvtkfdenlkktiermietmyhydgvglaapqvgisqrffvmdvgngpvavi npeileidpetevaeegclsfpeifveierskrikvkyqntrgeyveeelegyaarvfqhefdhlngvl iidrispakrlllrkklmdiartvkr | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 2 | | Resolution (Å) | 2.20 | Rfree | 0.249 | | Matthews' coefficent | 2.25 | Rfactor | 0.198 | | Waters | 103 | Solvent Content | 45.26 |
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
The gene TM1661 from Thermotoga maritima encodes polypeptide or peptide deformylase PF01327 E.C.3.5.1.88. The protein belongs to the class of alpha and beta (a+b) proteins and reveals peptide deformylase fold type SCOP56419. The enzyme belongs to a family of metalloenzymes that catalyzes the removal of the N-terminal formyl group in a growing polypeptide chain following translation initiation during protein synthesis in prokaryotes. These enzymes utilize Fe(II) as the catalytic metal ion, which can be replaced with a nickel or cobalt ion with no loss of activity. There are two types of peptide deformylases, types I and II, which differ in structure only in the outer surface of the domain. Because these enzymes are essential only in prokaryotes (although eukaryotic gene sequences have been found), they are a target for a new class of antibacterial agents [Ref]. The crystal structure of homologous enzyme from Plasmodium falciparum (malaria parasite) in complex with peptide-like inhibitor has been reported 1RL4.
Ligand Summary
References
