3V0H
Crystal structure of Ciona intestinalis voltage sensor-containing phosphatase (Ci-VSP), residues 241-576(C363S), complexed with D-MYO-inositol-1,4,5-triphosphate
Summary for 3V0H
| Entry DOI | 10.2210/pdb3v0h/pdb |
| Related | 3V0D 3V0E 3V0F 3V0G 3V0I 3V0J |
| Descriptor | Voltage-sensor containing phosphatase, D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | ptp, c2, phosphatase, hydrolase |
| Biological source | Ciona intestinalis (Transparent sea squirt) |
| Total number of polymer chains | 2 |
| Total formula weight | 79336.35 |
| Authors | Liu, L.,Kohout, S.C.,Xu, Q.,Muller, S.,Kimberlin, C.,Isacoff, E.Y.,Minor, D.L. (deposition date: 2011-12-08, release date: 2012-05-09, Last modification date: 2023-09-13) |
| Primary citation | Liu, L.,Kohout, S.C.,Xu, Q.,Muller, S.,Kimberlin, C.R.,Isacoff, E.Y.,Minor, D.L. A glutamate switch controls voltage-sensitive phosphatase function. Nat.Struct.Mol.Biol., 19:633-641, 2012 Cited by PubMed Abstract: The Ciona intestinalis voltage-sensing phosphatase (Ci-VSP) couples a voltage-sensing domain (VSD) to a lipid phosphatase that is similar to the tumor suppressor PTEN. How the VSD controls enzyme function has been unclear. Here, we present high-resolution crystal structures of the Ci-VSP enzymatic domain that reveal conformational changes in a crucial loop, termed the 'gating loop', that controls access to the active site by a mechanism in which residue Glu411 directly competes with substrate. Structure-based mutations that restrict gating loop conformation impair catalytic function and demonstrate that Glu411 also contributes to substrate selectivity. Structure-guided mutations further define an interaction between the gating loop and linker that connects the phosphatase to the VSD for voltage control of enzyme activity. Together, the data suggest that functional coupling between the gating loop and the linker forms the heart of the regulatory mechanism that controls voltage-dependent enzyme activation. PubMed: 22562138DOI: 10.1038/nsmb.2289 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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