1H, 13C, and 15N Chemical Shift Assignments for CutA1 from E. coli

Protonless 13C direct detection NMR: characterization of the 37 kDa trimeric protein CutA1.

Crystal Structure Of Cuta1 From E.Coli At 1.7 A Resolution

Crystal Structure Analysis Of The Mutant Cuta1 (S11vE61V) FROM E. Coli

Crystal Structure Analysis Of The Mutant Cuta1 (E61v) From E. Coli

Remarkable Improvement Of The Heat Stability Of Cuta1 From E.Coli By Rational Protein Designing

Crystal Structure Of Wild-type Of E. Coli Cuta1

Crystal Structure Of E.coli Cuta1 C16a/c39a/c79a Mutation

divalent cation tolerance protein CutA [Escherichia coli O157:H7 str. Sakai]

copper binding protein, copper sensitivity [Escherichia coli str. K12 substr. W3110]

copper binding protein, copper sensitivity [Escherichia coli O111:H-]

divalent cation tolerance protein [Escherichia coli SE11]

copper binding protein CutA, copper sensitivity [Escherichia coli O26:H11 str. 11368]

periplasmic divalent cation tolerance protein [Escherichia coli str. K-12 substr. W3110]

Divalent-cation tolerance protein cutA [Escherichia coli LF82]

copper binding protein CutA [Escherichia coli BL21(DE3)]

copper binding protein, copper sensitivity [Escherichia coli IAI1]

cycY [Escherichia coli str. K-12 substr. MG1655]

divalent-cation tolerance protein, copper sensitivity [Escherichia coli str. K-12 substr. MG1655]

divalent cation tolerance protein; cytochrome c biogenesis [Escherichia coli O157:H7 str. EDL933]

divalent cation tolerance protein [Shigella flexneri 2a str. 301]

Periplasmic divalent cation tolerance protein cutA [Escherichia coli CFT073]

divalent-cation tolerance protein CutA [Escherichia coli O157:H7 str. Sakai]

divalent-cation tolerance protein CutA [Shigella flexneri 2a str. 301]

divalent ion tolerance protein CutA [Escherichia coli]

RecName: Full=Divalent-cation tolerance protein CutA

We applied a combined strategy of 1H and 13C detection experiments to assigne
the trimeric protein CutA1 from E. coli. The CutA1 family of proteins is thought
to bind divalent metal ions and are present in archaea, bacteria, plants, and
animals. Their function is still unknown.
In this work we demonstrate that the unique information available from 13C
direct detection experiments makes it possible to assign the NMR resonances of
this 37 KDa protein without the need of deuteration.