Ligand-Induced Changes in the Structure and Dynamics of Escherichia coli Peptide Deformylase
Author:
Affiliation:
1. Biophysics Program
2. Biochemistry Program
3. Department of Biochemistry
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi900600b
Reference83 articles.
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3. Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion 1 1Edited by F. E. Cohen
4. Purification, Characterization, and Inhibition of Peptide Deformylase from Escherichia coli
5. Peptide Deformylase: A New Type of Mononuclear Iron Protein
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3. Understanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpart;Acta Crystallographica Section D Biological Crystallography;2014-01-17
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