3AWF
Crystal structure of Pten-like domain of Ci-VSP (236-576)
Summary for 3AWF
| Entry DOI | 10.2210/pdb3awf/pdb |
| Related | 3AWE 3AWG |
| Descriptor | Voltage-sensor containing phosphatase, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | ptdins(3, 4, 5)p3, phosphatase, ion channel, hydrolase, membrane protein |
| Biological source | Ciona intestinalis (Transparent sea squirt) |
| Total number of polymer chains | 3 |
| Total formula weight | 119678.09 |
| Authors | Matsuda, M.,Sakata, S.,Takeshita, K.,Suzuki, M.,Yamashita, E.,Okamura, Y.,Nakagawa, A. (deposition date: 2011-03-19, release date: 2011-05-04, Last modification date: 2024-10-30) |
| Primary citation | Matsuda, M.,Takeshita, K.,Kurokawa, T.,Sakata, S.,Suzuki, M.,Yamashita, E.,Okamura, Y.,Nakagawa, A. Crystal structure of the cytoplasmic phosphatase and tensin homolog (PTEN)-like region of Ciona intestinalis voltage-sensing phosphatase provides insight into substrate specificity and redox regulation of the phosphoinositide phosphatase activity J.Biol.Chem., 286:23368-23377, 2011 Cited by PubMed Abstract: Ciona intestinalis voltage-sensing phosphatase (Ci-VSP) has a transmembrane voltage sensor domain and a cytoplasmic region sharing similarity to the phosphatase and tensin homolog (PTEN). It dephosphorylates phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate upon membrane depolarization. The cytoplasmic region is composed of a phosphatase domain and a putative membrane interaction domain, C2. Here we determined the crystal structures of the Ci-VSP cytoplasmic region in three distinct constructs, wild-type (248-576), wild-type (236-576), and G365A mutant (248-576). The crystal structure of WT-236 and G365A-248 had the disulfide bond between the catalytic residue Cys-363 and the adjacent residue Cys-310. On the other hand, the disulfide bond was not present in the crystal structure of WT-248. These suggest the possibility that Ci-VSP is regulated by reactive oxygen species as found in PTEN. These structures also revealed that the conformation of the TI loop in the active site of the Ci-VSP cytoplasmic region was distinct from the corresponding region of PTEN; Ci-VSP has glutamic acid (Glu-411) in the TI loop, orienting toward the center of active site pocket. Mutation of Glu-411 led to acquirement of increased activity toward phosphatidylinositol 3,5-bisphosphate, suggesting that this site is required for determining substrate specificity. Our results provide the basic information of the enzymatic mechanism of Ci-VSP. PubMed: 21543329DOI: 10.1074/jbc.M110.214361 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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