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The Nucleotide Binding Protein 2(MinD homolog, E.coli)is a short form of NUBP family in Eukaryotes.the NUBP2 structure is 33.6% similar to 2ph1 which is a ligand binding protein from Archaeoglobus fulgidus. Basd on the structure of 2ph1, the research on the function and evolution of NUBP2 was conducted. the result shows that the NUBP2 contains the chracristic structure P-loop(the GXXXXGKT motif) which contributes to the ATP binding and have similar function with MinD ATPase which involved in cell division process. Futhermore, the evolution analysis also suggested that NUBP2 | The Nucleotide Binding Protein 2(MinD homolog, E.coli)is a short form of NUBP family in Eukaryotes.the NUBP2 structure is 33.6% similar to 2ph1 which is a ligand binding protein from Archaeoglobus fulgidus. Basd on the structure of 2ph1, the research on the function and evolution of NUBP2 was conducted. the result shows that the NUBP2 contains the chracristic structure P-loop(the GXXXXGKT motif) which contributes to the ATP binding and have similar function with MinD ATPase which involved in cell division process. Futhermore, the evolution analysis also suggested that NUBP2 | ||
is | is paralog to prokaryotic MRP and converged with E.Coli MinD, | ||
Revision as of 02:06, 10 June 2008
The Nucleotide Binding Protein 2(MinD homolog, E.coli)is a short form of NUBP family in Eukaryotes.the NUBP2 structure is 33.6% similar to 2ph1 which is a ligand binding protein from Archaeoglobus fulgidus. Basd on the structure of 2ph1, the research on the function and evolution of NUBP2 was conducted. the result shows that the NUBP2 contains the chracristic structure P-loop(the GXXXXGKT motif) which contributes to the ATP binding and have similar function with MinD ATPase which involved in cell division process. Futhermore, the evolution analysis also suggested that NUBP2 is paralog to prokaryotic MRP and converged with E.Coli MinD,
