2o9x

From Proteopedia

Revision as of 15:57, 20 March 2008

Crystal Structure Of A Putative Redox Enzyme Maturation Protein From Archaeoglobus Fulgidus

Overview

This paper describes the crystal structure of AF0173, a putative redox-enzyme maturation protein (REMP) from Archaeoglobus fulgidus. The REMPs serve as chaperones in the maturation of extracytoplasmic oxidoreductases in archaea and bacteria. The all-helical subunits of AF0173 form a dimer arising from the interaction of residues located in a funnel-shaped cavity on one subunit surface with an uncut expression tag from the other subunit. This cavity is likely to represent a binding site for the twin-arginine motif that interacts with REMPs. The conservation of the overall fold in AF0173 and bacterial REMPs as well as the presence of conserved residues in their putative binding sites indicates that REMPs act in a similar manner in archaea and bacteria despite their limited sequence similarity. A model of the binding of the twin-arginine motif by AF0173 is suggested. The solution of the AF0173 structure by the single anomalous dispersion method represents an extreme case of SAD structure determination: low resolution (3.4 A), the absence of NCS and the presence of only two anomalously scattering atoms in the asymmetric unit. An unusually high solvent content (73%) turned out to be important for the success of the density-modification procedures.

About this Structure

2O9X is a Single protein structure of sequence from Archaeoglobus fulgidus. This structure supersedes the now removed PDB entry 1ZE0. Full crystallographic information is available from OCA.

Reference

An extremely SAD case: structure of a putative redox-enzyme maturation protein from Archaeoglobus fulgidus at 3.4 A resolution., Kirillova O, Chruszcz M, Shumilin IA, Skarina T, Gorodichtchenskaia E, Cymborowski M, Savchenko A, Edwards A, Minor W, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):348-54. Epub 2007, Feb 21. PMID:17327672

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