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1.2 Å crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold
Author(s) -
Riboldi-Tunnicliffe A.,
Isaacs N.W.,
Mitchell T.J.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.08.066
Subject(s) - histidine , triad (sociology) , zinc , fold (higher order function) , chemistry , crystal structure , crystallography , biochemistry , amino acid , computer science , organic chemistry , psychology , psychoanalysis , programming language
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 Å using remote SAD with zinc. The structure of PhtA‐166–220 shows no similarity to any protein structure. The overall fold contains 3β‐strands and a single short α‐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.