The crystal structure of <Emphasis Type="Italic">Escherichia coli</Emphasis> TdcF,a member of the highly conserved YjgF/YER057c/UK114 family |
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| Authors: | Julia D Burman Clare EM Stevenson R Gary Sawers David M Lawson |
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| Institution: | 1.Department of Biological Chemistry,John Innes Centre,Norwich,UK;2.Department of Molecular Microbiology,John Innes Centre,Norwich,UK;3.Department of Biology and Biochemistry,University of Bath,Bath,UK;4.Max-Planck-Institut für Terrestrische Mikrobiologie,Karl-von-Frisch Strasse,Marburg,Germany |
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| Abstract: | Background The YjgF/YER057c/UK114 family of proteins is widespread in nature, but has as yet no clearly defined biological role. Members
of the family exist as homotrimers and are characterised by intersubunit clefts that are delineated by well-conserved residues;
these sites are likely to be of functional significance, yet catalytic activity has never been detected for any member of
this family. The gene encoding the TdcF protein of E. coli, a YjgF/YER057c/UK114 family member, resides in an operon that strongly suggests a role in the metabolism of 2-ketobutyrate
for this protein. |
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