Structure of free fumarase C from Escherichia coli.
Article Details
- CitationCopy to clipboard
Weaver T
Structure of free fumarase C from Escherichia coli.
Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1395-401. Epub 2005 Sep 28.
- PubMed ID
- 16204892 [ View in PubMed]
- Abstract
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.