2def

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(New page: 200px<br /> <applet load="2def" size="450" color="white" frame="true" align="right" spinBox="true" caption="2def" /> '''PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUE...)
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Revision as of 14:56, 29 October 2007


2def

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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 [[1]], with EC number [3.5.1.31]. 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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