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  Structure of peptide deformylase and identification of the substrate binding site

Becker, A., Schlichting, I., Kabsch, W., Schultz, S., & Wagner, A. F. V. (1998). Structure of peptide deformylase and identification of the substrate binding site. The Journal of Biological Chemistry, 273(19), 11413-11416. doi:10.1074/jbc.273.19.11413.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-7513-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-7514-4
Genre: Journal Article
Alternative Title : Structure of peptide deformylase and identification of the substrate binding site

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JBiolChem_273_1998_11413.pdf (Any fulltext), 417KB
 
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 Creators:
Becker, Andreas1, Author              
Schlichting, Ilme1, 2, Author              
Kabsch, Wolfgang1, 3, Author              
Schultz, Sabine, Author
Wagner, A. F. Volker, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society, ou_1856341              
3Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: Peptide deformylase is an essential metalloenzyme required for the removal of the formyl group at the N terminus of nascent polypeptide chains in eubacteria. The Escherichia coli enzyme uses Fe2+ and nearly retains its activity on substitution of the metal ion by Ni2+. We have solved the structure of the Ni2+ enzyme at 1.9-Å resolution by x-ray crystallography. Each of the three monomers in the asymmetric unit contains one Ni2+ ion and, in close proximity, one molecule of polyethylene glycol. Polyethylene glycol is shown to be a competitive inhibitor with a KI value of 6 mm with respect to formylmethionine under conditions similar to those used for crystallization. We have also solved the structure of the inhibitor-free enzyme at 2.5-Å resolution. The two structures are identical within the estimated errors of the models. The hydrogen bond network stabilizing the active site involves nearly all conserved amino acid residues and well defined water molecules, one of which ligates to the tetrahedrally coordinated Ni2+ion.

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Language(s): eng - English
 Dates: 1998-01-121998-05-08
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 273 (19) Sequence Number: - Start / End Page: 11413 - 11416 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1