2HET

Non-myristoylated bovine recoverin (truncated at C-terminus) with calcium bound to EF-hand 3

Summary for 2HET

• Entry DOI: 10.2210/pdb2het/pdb
• Descriptor: Recoverin, CALCIUM ION (2 entities in total)
• Functional Keywords: recoverin, ef-hand, helix-loop-helix, calcium binding, metal binding protein
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 4
• Total formula weight: 87153.60

Authors

Weiergraber, O.H.,Granzin, J. (deposition date: 2006-06-22, release date: 2006-10-17, Last modification date: 2023-08-30)

Primary citation

Weiergraber, O.H.,Senin, I.I.,Zernii, E.Y.,Churumova, V.A.,Kovaleva, N.A.,Nazipova, A.A.,Permyakov, S.E.,Permyakov, E.A.,Philippov, P.P.,Granzin, J.,Koch, K.W.
Tuning of a neuronal calcium sensor.
J.Biol.Chem., 281:37594-37602, 2006

PubMed Abstract: Recoverin is a Ca(2+)-regulated signal transduction modulator expressed in the vertebrate retina that has been implicated in visual adaptation. An intriguing feature of recoverin is a cluster of charged residues at its C terminus, the functional significance of which is largely unclear. To elucidate the impact of this segment on recoverin structure and function, we have investigated a mutant lacking the C-terminal 12 amino acids. Whereas in myristoylated recoverin the truncation causes an overall decrease in Ca(2+) sensitivity, results for the non-myristoylated mutant indicate that the truncation primarily affects the high affinity EF-hand 3. The three-dimensional structure of the mutant has been determined by x-ray crystallography. In addition to significant changes in average coordinates compared with wild-type recoverin, the structure provides strong indication of increased conformational flexibility, particularly in the C-terminal domain. Based on these observations, we propose a novel role of the C-terminal segment of recoverin as an internal modulator of Ca(2+) sensitivity.

PubMed: 17015448
DOI: 10.1074/jbc.M603700200

Experimental method

X-RAY DIFFRACTION (3 Å)