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Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1395-401. Epub 2005 Sep 28.

Structure of free fumarase C from Escherichia coli.

Author information

1
Department of Chemistry, University of Wisconsin-La Crosse, 1725 State Street, 4020 Cowley Hall, La Crosse, Wisconsin 54601, USA. weaver.todd@uwlax.edu

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.

PMID:
16204892
DOI:
10.1107/S0907444905024194
[Indexed for MEDLINE]

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