1YGP
PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.
Summary for 1YGP
| Entry DOI | 10.2210/pdb1ygp/pdb |
| Descriptor | YEAST GLYCOGEN PHOSPHORYLASE, PHOSPHATE ION, PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
| Functional Keywords | yeast, phosphorylated form, glycosyltransferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 203431.81 |
| Authors | Lin, K.,Rath, V.L.,Dai, S.C.,Fletterick, R.J.,Hwang, P.K. (deposition date: 1996-05-30, release date: 1996-12-23, Last modification date: 2024-06-05) |
| Primary citation | Lin, K.,Rath, V.L.,Dai, S.C.,Fletterick, R.J.,Hwang, P.K. A protein phosphorylation switch at the conserved allosteric site in GP. Science, 273:1539-1542, 1996 Cited by PubMed Abstract: A phosphorylation-initiated mechanism of local protein refolding activates yeast glycogen phosphorylase (GP). Refolding of the phosphorylated amino-terminus was shown to create a hydrophobic cluster that wedges into the subunit interface of the enzyme to trigger activation. The phosphorylated threonine is buried in the allosteric site. The mechanism implicates glucose 6-phosphate, the allosteric inhibitor, in facilitating dephosphorylation by dislodging the buried covalent phosphate through binding competition. Thus, protein phosphorylation-dephosphorylation may also be controlled through regulation of the accessibility of the phosphorylation site to kinases and phosphatases. In mammalian glycogen phosphorylase, phosphorylation occurs at a distinct locus. The corresponding allosteric site binds a ligand activator, adenosine monophosphate, which triggers activation by a mechanism analogous to that of phosphorylation in the yeast enzyme. PubMed: 8703213PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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