1YX7

NMR structure of Calsensin, energy minimized average structure.

Summary for 1YX7

• Entry DOI: 10.2210/pdb1yx7/pdb
• Related: 1YX8
• NMR Information: BMRB: 6519
• Descriptor: Calsensin (1 entity in total)
• Functional Keywords: calsensin, calcium-binding protein ef-hand, helix-loop-helix, nervous system, metal binding protein
• Biological source: Haemopis marmorata
• Cellular location: Cytoplasm: Q25088
• Total number of polymer chains: 1
• Total formula weight: 9115.63

Authors

Venkitaramani, D.V.,Fulton, D.B.,Andreotti, A.H.,Johansen, K.M.,Johansen, J. (deposition date: 2005-02-19, release date: 2005-04-01, Last modification date: 2024-05-22)

Primary citation

Venkitaramani, D.V.,Fulton, D.B.,Andreotti, A.H.,Johansen, K.M.,Johansen, J.
Solution structure and backbone dynamics of Calsensin, an invertebrate neuronal calcium-binding protein.
Protein Sci., 14:1894-1901, 2005

PubMed Abstract: Calsensin is an EF-hand calcium-binding protein expressed by a subset of peripheral sensory neurons that fasciculate into a single tract in the leech central nervous system. Calsensin is a 9-kD protein with two EF-hand calcium-binding motifs. Using multidimensional NMR spectroscopy we have determined the solution structure and backbone dynamics of calcium-bound Calsensin. Calsensin consists of four helices forming a unicornate-type four-helix bundle. The residues in the third helix undergo slow conformational exchange indicating that the motion of this helix is associated with calciumbinding. The backbone dynamics of the protein as measured by (15)N relaxation rates and heteronuclear NOEs correlate well with the three-dimensional structure. Furthermore, comparison of the structure of Calsensin with other members of the EF-hand calcium-binding protein family provides insight into plausible mechanisms of calcium and target protein binding.

PubMed: 15937283
DOI: 10.1110/ps.051412605

Experimental method

SOLUTION NMR