2DEF

PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1-147), NMR, 20 STRUCTURES

2DEF の概要

• エントリーDOI: 10.2210/pdb2def/pdb
• NMR情報: BMRB: 4089
• 分子名称: PEPTIDE DEFORMYLASE, NICKEL (II) ION (2 entities in total)
• 機能のキーワード: hydrolase, metalloprotease
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16703.82

構造登録者

Meinnel, T.,Dardel, F. (登録日: 1997-12-15, 公開日: 1998-03-18, 最終更新日: 2024-05-22)

主引用文献

Dardel, F.,Ragusa, S.,Lazennec, C.,Blanquet, S.,Meinnel, T.
Solution structure of nickel-peptide deformylase.
J.Mol.Biol., 280:501-513, 1998

PubMed Abstract: In the accompanying paper, we report that zinc is unlikely to be the co-factor supporting peptide deformylase activity in vivo. In contrast, nickel binding promotes full enzyme activity. The three-dimensional structure of the resulting nickel-containing peptide deformylase (catalytic domain, residues 1 to 147) was solved by NMR using a 13C-15N-doubly labelled protein sample. A set of 2261 restraints could be collected, with an average of 15.4 per amino acid. The resolution, which shows a good definition for the position of most side-chains, is greatly improved compared to that previously reported for the zinc-containing, inactive form. A comparison of the two stuctures indicates however that both share the same 3D organization. This shows that the nature of the bound metal is the primary determinant of the hydrolytic activity of this enzyme. Site-directed mutagenesis enabled us to determine the conserved residues of PDF involved in the structure of the active site. In particular, a buried arginine appears to be critical for the positioning of Cys90, one of the metal ligands. Furthermore, the 3D structure of peptide deformylase was compared to thermolysin and metzincins. Although the structural folds are very different, they all display a common structural motif involving an alpha-helix and a three-stranded beta-sheet. These conserved structural elements build a common scaffold which includes the active site, suggesting a common hydrolytic mechanism for these proteases. Finally, an invariant glycine shared by both PDF and metzincins enables us to extend the conserved motif from HEXXH to HEXXHXXG.

PubMed: 9665852
DOI: 10.1006/jmbi.1998.1882

実験手法

SOLUTION NMR