1c7w
From Proteopedia
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| - | [[Image:1c7w.gif|left|200px]] | + | [[Image:1c7w.gif|left|200px]] |
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| - | '''NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS''' | + | {{Structure |
| + | |PDB= 1c7w |SIZE=350|CAPTION= <scene name='initialview01'>1c7w</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1C7W is a [ | + | 1C7W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Branchiostoma_lanceolatum Branchiostoma lanceolatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C7W OCA]. |
==Reference== | ==Reference== | ||
| - | Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement., Theret I, Baladi S, Cox JA, Sakamoto H, Craescu CT, Biochemistry. 2000 Jul 11;39(27):7920-6. PMID:[http:// | + | Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement., Theret I, Baladi S, Cox JA, Sakamoto H, Craescu CT, Biochemistry. 2000 Jul 11;39(27):7920-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10891072 10891072] |
[[Category: Branchiostoma lanceolatum]] | [[Category: Branchiostoma lanceolatum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nmr]] | [[Category: nmr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:21:05 2008'' |
Revision as of 08:21, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS
Overview
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.
About this Structure
1C7W is a Single protein structure of sequence from Branchiostoma lanceolatum. Full crystallographic information is available from OCA.
Reference
Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement., Theret I, Baladi S, Cox JA, Sakamoto H, Craescu CT, Biochemistry. 2000 Jul 11;39(27):7920-6. PMID:10891072
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