PDBsum entry 4m2q

Metal binding protein

PDB id: 4m2q

Contents

Protein chain

188 a.a.

Metals

_CA

Waters ×115

PDB id:

4m2q

Name:

Metal binding protein

Title:

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

Structure:

Recoverin. Chain: a. Synonym: p26. Engineered: yes

Source:

Bos taurus. Bovine,cow,domestic cattle,domestic cow. Organism_taxid: 9913. Gene: rcv1, rcvrn, recoverin. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.90Å R-factor: 0.191 R-free: 0.221

Authors:

R.Prem Kumar,K.Chakrabarti,D.Kern,D.D.Oprian

Key ref:

M.J.Ranaghan et al. (2013). A highly conserved cysteine of neuronal calcium-sensing proteins controls cooperative binding of Ca2+ to recoverin. J Biol Chem, 288, 36160-36167. PubMed id: 24189072 DOI: 10.1074/jbc.M113.524355

Date:

05-Aug-13 Release date: 13-Nov-13

Protein chain

P21457  (RECO_BOVIN) -  Recoverin from Bos taurus

Seq: 202 a.a.

Struc: 188 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1074/jbc.M113.524355

J Biol Chem 288:36160-36167 (2013)

PubMed id: 24189072

A highly conserved cysteine of neuronal calcium-sensing proteins controls cooperative binding of Ca2+ to recoverin.

M.J.Ranaghan, R.P.Kumar, K.S.Chakrabarti, V.Buosi, D.Kern, D.D.Oprian.

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.