3E3U

Crystal structure of Mycobacterium tuberculosis peptide deformylase in complex with inhibitor

Summary for 3E3U

• Entry DOI: 10.2210/pdb3e3u/pdb
• Descriptor: Peptide deformylase, NICKEL (II) ION, N-[(2R)-2-{[(2S)-2-(1,3-benzoxazol-2-yl)pyrrolidin-1-yl]carbonyl}hexyl]-N-hydroxyformamide, ... (4 entities in total)
• Functional Keywords: metallo-enzyme, hydrolase, iron, metal-binding, protein biosynthesis
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 22096.64

Authors

Meng, W.,Xu, M.,Pan, S.,Koehn, J. (deposition date: 2008-08-08, release date: 2009-01-20, Last modification date: 2024-02-21)

Primary citation

Pichota, A.,Duraiswamy, J.,Yin, Z.,Keller, T.H.,Alam, J.,Liung, S.,Lee, G.,Ding, M.,Wang, G.,Chan, W.L.,Schreiber, M.,Ma, I.,Beer, D.,Ngew, X.,Mukherjee, K.,Nanjundappa, M.,Teo, J.W.,Thayalan, P.,Yap, A.,Dick, T.,Meng, W.,Xu, M.,Koehn, J.,Pan, S.H.,Clark, K.,Xie, X.,Shoen, C.,Cynamon, M.
Peptide deformylase inhibitors of Mycobacterium tuberculosis: synthesis, structural investigations, and biological results.
Bioorg.Med.Chem.Lett., 18:6568-6572, 2008

PubMed Abstract: Bacterial peptide deformylase (PDF) belongs to a subfamily of metalloproteases catalyzing the removal of the N-terminal formyl group from newly synthesized proteins. We report the synthesis and biological activity of highly potent inhibitors of Mycobacterium tuberculosis (Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure-activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported.

PubMed: 19008098
DOI: 10.1016/j.bmcl.2008.10.040

Experimental method

X-RAY DIFFRACTION (1.56 Å)