2ZKM
Crystal Structure of Phospholipase C Beta 2
Summary for 2ZKM
| Entry DOI | 10.2210/pdb2zkm/pdb |
| Descriptor | 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2, CALCIUM ION (3 entities in total) |
| Functional Keywords | phospholipase c, phosphoinositide phospholipase, plc-beta-2, calcium, coiled coil, hydrolase, lipid degradation, metal-binding, transducer |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 91074.00 |
| Authors | Hicks, S.N.,Jezyk, M.R.,Gershberg, S.,Seifert, J.P.,Harden, T.K.,Sondek, J. (deposition date: 2008-03-26, release date: 2008-08-12, Last modification date: 2023-11-01) |
| Primary citation | Hicks, S.N.,Jezyk, M.R.,Gershburg, S.,Seifert, J.P.,Harden, T.K.,Sondek, J. General and versatile autoinhibition of PLC isozymes Mol.Cell, 31:383-394, 2008 Cited by PubMed Abstract: Phospholipase C (PLC) isozymes are directly activated by heterotrimeric G proteins and Ras-like GTPases to hydrolyze phosphatidylinositol 4,5-bisphosphate into the second messengers diacylglycerol and inositol 1,4,5-trisphosphate. Although PLCs play central roles in myriad signaling cascades, the molecular details of their activation remain poorly understood. As described here, the crystal structure of PLC-beta2 illustrates occlusion of the active site by a loop separating the two halves of the catalytic TIM barrel. Removal of this insertion constitutively activates PLC-beta2 without ablating its capacity to be further stimulated by classical G protein modulators. Similar regulation occurs in other PLC members, and a general mechanism of interfacial activation at membranes is presented that provides a unifying framework for PLC activation by diverse stimuli. PubMed: 18691970DOI: 10.1016/j.molcel.2008.06.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.62 Å) |
Structure validation
Download full validation report
