NUBP2E: Difference between revisions

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Structural, functional and evolutionary analyses collectively indicate that Nucleotide Binding Protein 2 (MinD homolog, E.coli) is one of the membrane associated ATPase family. It involved in cell division to determine the position of septum (Z-ring) though the MinD complex. Prokaryotic MRP proteins and eukaryotic nucleotide binding proteins (NBP) are paralogs that share a common ancestral gene but possess different functions. Many NBPs contain the highly conserved structure P-loop (MRP-like) that acts as an ATPase. There are two subtypes of NBP in eukarytes, NBP1 appeared earlier in evolution than NBP2.  The origination of NBP2 was likely achieved by the deletion of the Cysteine-rich N-terminal of NBP1.
Structural, functional and evolutionary analyses collectively indicate that Nucleotide Binding Protein 2 (MinD homolog, E.coli) is one of the membrane associated ATPase family. It involved in cell division to determine the position of septum (Z-ring) though the MinD complex. NUBP2 is the paralog to prokaryotic MRP proteins; converged with bacterial MinD; and orginated from NUBP1.

Latest revision as of 01:39, 10 June 2008

Structural, functional and evolutionary analyses collectively indicate that Nucleotide Binding Protein 2 (MinD homolog, E.coli) is one of the membrane associated ATPase family. It involved in cell division to determine the position of septum (Z-ring) though the MinD complex. NUBP2 is the paralog to prokaryotic MRP proteins; converged with bacterial MinD; and orginated from NUBP1.

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