1c7w

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|ACTIVITY=
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|RELATEDENTRY=[[1c7v|1C7V]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c7w OCA], [http://www.ebi.ac.uk/pdbsum/1c7w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c7w RCSB]</span>
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[[Category: nmr]]
[[Category: nmr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:16:23 2008''

Revision as of 16:16, 30 March 2008


PDB ID 1c7w

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Related: 1C7V


Resources: FirstGlance, OCA, PDBsum, RCSB
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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