1C7V
NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS
Summary for 1C7V
| Entry DOI | 10.2210/pdb1c7v/pdb |
| Related | 1C7W |
| Descriptor | CALCIUM VECTOR PROTEIN (1 entity in total) |
| Functional Keywords | ef-hand family, calcium binding protein, metal binding protein |
| Biological source | Branchiostoma lanceolatum (amphioxus) |
| Cellular location | Cytoplasm: P04573 |
| Total number of polymer chains | 1 |
| Total formula weight | 9279.27 |
| Authors | Theret, I.,Baladi, S.,Cox, J.A.,Sakamoto, H.,Craescu, C.T. (deposition date: 2000-03-27, release date: 2000-04-12, Last modification date: 2023-12-27) |
| Primary citation | Theret, I.,Baladi, S.,Cox, J.A.,Sakamoto, H.,Craescu, C.T. Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement. Biochemistry, 39:7920-7926, 2000 Cited by PubMed Abstract: Calcium vector protein (CaVP) from amphioxus is a two-domain, calcium-binding protein (18.3 kDa) of the calmodulin superfamily. Only two of the four EF-hand motifs (sites III and IV) have a significant binding affinity for calcium ions. We determined the solution structure of the domain containing these active sites (C-CaVP: W81-S161), in the Ca(2+)-saturated state, using NMR spectroscopy and restrained molecular dynamics. The tertiary structure is similar to other Ca(2+)-binding domains containing a pair of EF-hand motifs. The apo state has spectroscopic and thermodynamic characteristics of a molten globule, with conserved secondary structure but highly fluctuating tertiary organization. Titration of C-CaVP with Ca(2+) revealed a stepwise ion binding, with a stable equilibrium intermediate in which only site III binds a calcium ion. Despite a highly fluctuating structure of the free site IV, the calcium-bound site III has a persistent structure, with similar secondary elements but different interhelix angle and hydrophobic packing relative to the fully calcium-saturated state. PubMed: 10891072DOI: 10.1021/bi000360z PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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