P-loop

From Wikipedia, the free encyclopedia

Alignment of the H-Ras mutant A59G mutants in complex with GppNHp (green cartoon) and GDP (cyan cartoon). The P-loop main chain is shown in red, the Mg2+ ion as green sphere and the side chains of the amino acids K16 and S17 are shown as sticks.
Alignment of the H-Ras mutant A59G mutants in complex with GppNHp (green cartoon) and GDP (cyan cartoon). The P-loop main chain is shown in red, the Mg2+ ion as green sphere and the side chains of the amino acids K16 and S17 are shown as sticks.

A P-loop or phosphate-binding loop, is an ATP/GTP binding site motif found in many nucleotide-binding proteins. It is a glycine-rich loop preceded by a β-sheet and followed by an α-helix. It interacts with the phosphate groups of the nucleotide and the Mg2+ ion, which coordinates the β- and the γ-phosphate.

The consensus sequence of the P-loop is GxxxxGK(S/T), which is often referred to as Walker A motif. Upon nucleotide hydrolysis the P-loop does not change its conformation significantly, it rather stays bound to the remaining phosphate groups.

Proteins with (functional) P-loops include ATP synthase, myosin, transducin, helicase and Small GTPases like Ras.

PTPs (Protein tyrosine phosphatases) which catalyse the hydrolysis of an inorganic phosphate from a phosphotyrosine residue (see Tyrosine kinase) also contain a P-loop-similar motif. The conserved sequence of this motif is CxxxxxR(S/T)

[edit] See also

[edit] References

Stryer, L.; Berg, J. M.; Tymoczko, J. L. (2002). Biochemistry, 5th Ed., New York: W. H. Freeman. ISBN 0716746840.  Searchable text

Walker,J.E., Saraste,M., Runswick,M.J. and Gay,N.J. (1982) EMBO J., 1, 945–951 Full-text article at pubmedcentral.