PDBsum entry 4yi9

Calcium binding protein

PDB id: 4yi9

Contents

Protein chain

192 a.a.

Metals

_CA

_NA

Waters ×232

PDB id:

4yi9

Name:

Calcium binding protein

Title:

Crystal structure of non-myristoylated e153a recoverin at 1.35 a resolution with a sodium ion bound to ef-hand 2 and calcium ion bound to ef-hand 3

Structure:

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

Source:

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

Resolution:

1.35Å R-factor: 0.153 R-free: 0.174

Authors:

R.Prem Kumar,M.J.Ranaghan,D.D.Oprian

Key ref:

R.P.Kumar et al. (2015). Crystal Structure of Recoverin with Calcium Ions Bound to Both Functional EF Hands. Biochemistry, 54, 7222-7228. PubMed id: 26584024 DOI: 10.1021/acs.biochem.5b01160

Date:

28-Feb-15 Release date: 02-Dec-15

Protein chain

P21457  (RECO_BOVIN) -  Recoverin from Bos taurus

Seq: 202 a.a.

Struc: 192 a.a.*

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

DOI no: 10.1021/acs.biochem.5b01160

Biochemistry 54:7222-7228 (2015)

PubMed id: 26584024

Crystal Structure of Recoverin with Calcium Ions Bound to Both Functional EF Hands.

R.P.Kumar, M.J.Ranaghan, A.Y.Ganjei, D.D.Oprian.

ABSTRACT

Recoverin (Rv), a small Ca(2+)-binding protein that inhibits rhodopsin kinase (RK), has four EF hands, two of which are functional (EF2 and EF3). Activation requires Ca(2+) in both EF hands, but crystal structures have never been observed with Ca(2+) ions in both sites; all previous structures have Ca(2+) bound to only EF3. We suspected that this was due to an intermolecular crystal contact between T80 and a surface glutamate (E153) that precluded coordination of a Ca(2+) ion in EF2. We constructed the E153A mutant, determined its X-ray crystal structure to 1.2 Å resolution, and showed that two Ca(2+) ions are bound, one in EF3 and one in EF2. Additionally, several other residues are shown to adopt conformations in the 2Ca(2+) structure not seen previously and not seen in a second structure of the E153A mutant containing Na(+) instead of Ca(2+) in the EF2 site. The side-chain rearrangements in these residues form a 28 Å allosteric cascade along the surface of the protein connecting the Ca(2+)-binding site of EF2 with the active-site pocket responsible for binding RK.