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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 

Structure of free fumarase C from Escherichia coli.

Previous crystal structures of fumarase C from Escherichia coli have noted two occupied dicarboxylate-binding sites termed the active site and the B site. Here, the first known fumarase C structure is reported in which both sites are unoccupied by bound ligand. This so-called ;free' crystal form shows conservation of the active-site water in a similar orientation to that reported in other fumarase C crystal structures. More importantly, a shift of His129 has been observed at the B site. This new crystallographic information suggests the use of water as a permanent member of the active site and the use of an imidazole-imidazolium conversion to control access at the allosteric B site.[1]

References

  1. Structure of free fumarase C from Escherichia coli. Weaver, T. Acta Crystallogr. D Biol. Crystallogr. (2005) [Pubmed]
 
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