2cs7
From Proteopedia
1.2 A Crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold
Overview
The recently described pneumococcal histidine triad protein family has been shown to be highly conserved within the pneumococcus. As part of our structural genomics effort on proteins from Streptococcus pneumoniae, we have expressed, crystallised and solved the structure of PhtA-166-220 at 1.2 Angstroms using remote SAD with zinc. The structure of PhtA-166-220 shows no similarity to any protein structure. The overall fold contains 3beta-strands and a single short alpha-helix. The structure appears to contain a novel zinc binding motif. The remaining 4 histidine triad repeats from PhtA have been modelled based on the crystal structure of the PhtA histidine triad repeat 2. From this modelling work, we speculate that only three of the five histidine triad repeats contain the residues in the correct geometry to allow the binding of a zinc ion.
About this Structure
2CS7 is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
Reference
1.2 Angstroms crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold., Riboldi-Tunnicliffe A, Isaacs NW, Mitchell TJ, FEBS Lett. 2005 Oct 10;579(24):5353-60. PMID:16194532 Page seeded by OCA on Sat May 3 22:55:55 2008
