4M2Q

Crystal structure of non-myristoylated recoverin with Cysteine-39 oxidized to sulfenic acid

Summary for 4M2Q

• Entry DOI: 10.2210/pdb4m2q/pdb
• Related: 1OMR 4M2O 4M2P 4MLW
• Descriptor: Recoverin, CALCIUM ION (3 entities in total)
• Functional Keywords: calcium binding protein, ef hand, neuronal calcium sensing (ncs) family protein, inhibits rhodopsin kinase, rhodopsin kinase, retina, metal binding protein
• Biological source: Bos taurus (bovine,cow,domestic cattle,domestic cow)
• Total number of polymer chains: 1
• Total formula weight: 23291.29

Authors

Prem Kumar, R.,Chakrabarti, K.,Kern, D.,Oprian, D.D. (deposition date: 2013-08-05, release date: 2013-11-13, Last modification date: 2023-09-20)

Primary citation

Ranaghan, M.J.,Kumar, R.P.,Chakrabarti, K.S.,Buosi, V.,Kern, D.,Oprian, D.D.
A Highly Conserved Cysteine of Neuronal Calcium-sensing Proteins Controls Cooperative Binding of Ca2+ to Recoverin.
J.Biol.Chem., 288:36160-36167, 2013

PubMed Abstract: Recoverin, a 23-kDa Ca(2+)-binding protein of the neuronal calcium sensing (NCS) family, inhibits rhodopsin kinase, a Ser/Thr kinase responsible for termination of photoactivated rhodopsin in rod photoreceptor cells. Recoverin has two functional EF hands and a myristoylated N terminus. The myristoyl chain imparts cooperativity to the Ca(2+)-binding sites through an allosteric mechanism involving a conformational equilibrium between R and T states of the protein. Ca(2+) binds preferentially to the R state; the myristoyl chain binds preferentially to the T state. In the absence of myristoylation, the R state predominates, and consequently, binding of Ca(2+) to the non-myristoylated protein is not cooperative. We show here that a mutation, C39A, of a highly conserved Cys residue among NCS proteins, increases the apparent cooperativity for binding of Ca(2+) to non-myristoylated recoverin. The binding data can be explained by an effect on the T/R equilibrium to favor the T state without affecting the intrinsic binding constants for the two Ca(2+) sites.

PubMed: 24189072
DOI: 10.1074/jbc.M113.524355

Experimental method

X-RAY DIFFRACTION (1.9 Å)