1YFE

Crystal structure of apo fumarase C from Escherichia coli

Summary for 1YFE

Entry DOI	10.2210/pdb1yfe/pdb
Related	1FUO 1FUP 1FUQ
Descriptor	Fumarate hydratase class II (2 entities in total)
Functional Keywords	fumarase, kreb's cycle, apo, allosteric, lyase
Biological source	Escherichia coli
Cellular location	Cytoplasm : P05042
Total number of polymer chains	1
Total formula weight	50548.77
Authors	Weaver, T. (deposition date: 2004-12-31, release date: 2005-10-18, Last modification date: 2023-08-23)
Primary citation	Weaver, T. Structure of free fumarase C from Escherichia coli. Acta Crystallogr.,Sect.D, 61:1395-1401, 2005 Cited by 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. PubMed: 16204892 DOI: 10.1107/S0907444905024194 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.19 Å)

Structure validation