Abstract
Structure of Escherichia coli UMP Kinase Differs from That ofOther Nucleoside Monophosphate Kinases and Sheds New Light on EnzymeRegulation
Highlights
Nucleoside monophosphate kinases are key enzymes in the metabolism of nucleotides
A Nucleoside Monophosphate Kinase with an Atypical Regulation Supported by an Atypical Fold—UMP kinase from E. coli (UMPKeco) exhibits striking differences with other NMP kinases concerning its activity regulation: activation by the GTP effector and inhibition by UTP, the end product of the phosphorylation pathway
The monomer fold of UMPKeco is close to that of NAGK and CBMK, which suggests that these three kinases derive from a common ancestor
Summary
Chemicals—Nucleotides, restriction enzymes, T4 DNA ligase, VentDNA polymerase, Tfu DNA polymerase, and coupling enzymes were from Roche Applied Science, Sigma, or Qbiogene. The drop contained ADPNP in the case of UMP- (25 mM, in the presence of 25 mM MgCl2) and UTP-containing complexes (5 mM), but this ATP analogue was not seen later in the corresponding electron density maps. The structures of UMP- and UDP-UMPKeco complexes were solved by molecular replacement at 3.5 Å resolution with AMoRe (19), using only the protein part of the UTP-UMPKeco model. In both cases, a clear density immediately appeared for the nucleotide. The Protein Data Bank codes of the E. coli UMPK complexes are 2BNE with UMP, 2BND with UDP, and 2BNF with UTP
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
