PDBsum entry 1omv

Metal binding protein

PDB id: 1omv

Contents

Protein chain

188 a.a. *

Metals

_CA

Waters ×76

* Residue conservation analysis

PDB id:

1omv

Name:

Metal binding protein

Title:

Non-myristoylated bovine recoverin (e85q mutant) with calcium bound to ef-hand 3

Structure:

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

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Gene: rcv1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Tetramer (from PQS)

Resolution:

1.90Å R-factor: 0.240 R-free: 0.249

Authors:

O.H.Weiergraber,J.Granzin

Key ref:

O.H.Weiergräber et al. (2003). Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin. J Biol Chem, 278, 22972-22979. PubMed id: 12686556 DOI: 10.1074/jbc.M300447200

Date:

26-Feb-03 Release date: 25-Nov-03

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.M300447200

J Biol Chem 278:22972-22979 (2003)

PubMed id: 12686556

Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin.

O.H.Weiergräber, I.I.Senin, P.P.Philippov, J.Granzin, K.W.Koch.

ABSTRACT

Recoverin is a Ca2+-regulated signal transduction modulator found in vertebrate retina that has been shown to undergo dramatic conformational changes upon Ca2+ binding to its two functional EF-hand motifs. To elucidate the differential impact of the N-terminal myristoylation as well as occupation of the two Ca2+ binding sites on recoverin structure and function, we have investigated a non-myristoylated E85Q mutant exhibiting virtually no Ca2+ binding to EF-2. Crystal structures of the mutant protein as well as the non-myristoylated wild-type have been determined. Although the non-myristoylated E85Q mutant does not display any functional activity, its three-dimensional structure in the presence of Ca2+ resembles the myristoylated wild-type with two Ca2+ but is quite dissimilar from the myristoylated E85Q mutant. We conclude that the N-terminal myristoyl modification significantly stabilizes the conformation of the Ca2+-free protein (i.e. the T conformation) during the stepwise transition toward the fully Ca2+-occupied state. On the basis of these observations, a refined model for the role of the myristoyl group as an intrinsic allosteric modulator is proposed.

Selected figure(s)

Figure 7.
FIG. 7. Arrangement of side chains critical for interaction with rhodopsin kinase (as defined in Ref. 41). Residues probably involved in the binding interface according to these authors are colored in red, those of minor significance in orange. Abbreviations are as in Fig. 6.

Figure 8.
FIG. 8. C[ ]trace superposition (identical to Fig. 5 with 180° rotation) of non-myristoylated recoverin with one Ca^2+ (darker colors) and myristoylated recoverin with two Ca^2+ (lighter colors) showing positional re-arrangement of hydrophobic residues forming the patch defined in Fig. 6 (yellow backbone) and of side chains probably (light and dark red) and possibly (light and dark orange) involved in rhodopsin kinase inhibition (see Fig. 7).

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 22972-22979) copyright 2003.

Figures were selected by an automated process.