2CS7

1.2 A Crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold

Summary for 2CS7

• Entry DOI: 10.2210/pdb2cs7/pdb
• Descriptor: pneumococcal histidine triad A protein, ZINC ION (3 entities in total)
• Functional Keywords: phta, pneumococcal histidine triad protein, s.pneumoniae, structural genomics, unknown function
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 3
• Total formula weight: 18272.45

Authors

Riboldi-Tunnicliffe, A.,Isaacs, N.W.,Mitchell, T.J. (deposition date: 2005-05-20, release date: 2006-02-14, Last modification date: 2024-02-14)

Primary citation

Riboldi-Tunnicliffe, A.,Isaacs, N.W.,Mitchell, T.J.
1.2 Angstroms crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold.
Febs Lett., 579:5353-5360, 2005

PubMed Abstract: 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.

PubMed: 16194532
DOI: 10.1016/j.febslet.2005.08.066

Experimental method

X-RAY DIFFRACTION (1.2 Å)