2def
From Proteopedia
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PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1-147), NMR, 20 STRUCTURES
Overview
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 ... [(full description)]
About this Structure
2DEF is a [Single protein] structure of sequence from [Escherichia coli] with NI as [ligand]. Active as [Formylmethionine deformylase], with EC number [3.5.1.31]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
Solution structure of nickel-peptide deformylase., Dardel F, Ragusa S, Lazennec C, Blanquet S, Meinnel T, J Mol Biol. 1998 Jul 17;280(3):501-13. PMID:9665852
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