Structure Myosin-light-chain phosphatase

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a 3d representation of pp1 (shown in red) , portion of mypt1 (shown in blue), manganese ion catalysts shown in white. yellow lines mark grooves critical enzyme binding , catalysis.


myosin phosphatase made of 3 subunits. catalytic subunit, pp1, 1 of more important ser/thr phosphatases in eukaryotic cells, plays role in glycogen metabolism, intracellular transport, protein synthesis, , cell division smooth muscle contraction. because important basic cellular functions, , because there far fewer protein phosphatases kinases in cells, pp1’s structure , function highly conserved (though specific isoform used in myosin phosphatase δ isoform, pp1δ). pp1 works using 2 manganese ions catalysts dephosphorylation (see below).


surrounding these ions y-shaped cleft 3 grooves: hydrophobic, acidic, , c-terminal groove. when pp1 not bonded other subunit, not particularly specific. however, when bonds second subunit of myosin phosphatase, mypt1 (mw ~130 kda), catalytic cleft changes configuration. results in dramatic increase in myosin specificity. thus, clear mypt1 has great regulatory power on pp1 , myosin phosphatase, without presence of other activators or inhibitors.


the third subunit, m20 (not confused mlc20, critical regulatory subunit of myosin), smallest , mysterious subunit. little known m20, except not necessary catalysis, removing subunit not affect turnover or selectivity. while believe have regulatory function, nothing has been determined yet.








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