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<font size = "5">'''Abstract'''</font>
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,
 
''N''-acetylneuraminic acid phosphatase a novel protein investigated by our group. With its structure and sequence known, the function was  
 
assumed to be a part of the enormous family of haloacid dehalogenase-like hydrolases. It represent the family of predicted small molecule
 
phosphatases related by sequence cleave sites and reactions in the genomes of bacteria, archaea, and eukaryotes. Many have evolved to be used
 
for specific biological functions within individual organism

Latest revision as of 07:37, 2 June 2009

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,