PDBsum entry 5eet

Transport protein

PDB id: 5eet

Contents

Protein chain

148 a.a.

Ligands

HEM

SO4

Waters ×76

PDB id:

5eet

Name:

Transport protein

Title:

Crystal structure of murine neuroglobin at ambient pressure

Structure:

Neuroglobin. Chain: a. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: ngb. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss.

Resolution:

2.00Å R-factor: 0.145 R-free: 0.181

Authors:

N.Colloc'H,E.Girard,B.Vallone

Key ref:

N.Colloc'h et al. (2017). Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography. Sci Rep, 7, 1858. PubMed id: 28500341

Date:

23-Oct-15 Release date: 19-Oct-16

Protein chain

Q9ER97  (NGB_MOUSE) -  Neuroglobin from Mus musculus

Seq: 151 a.a.

Struc: 148 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Sci Rep 7:1858 (2017)

PubMed id: 28500341

Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography.

N.Colloc'h, S.Sacquin-Mora, G.Avella, A.C.Dhaussy, T.Prangé, B.Vallone, E.Girard.

ABSTRACT

Investigating the effect of pressure sheds light on the dynamics and plasticity of proteins, intrinsically correlated to functional efficiency. Here we detail the structural response to pressure of neuroglobin (Ngb), a hexacoordinate globin likely to be involved in neuroprotection. In murine Ngb, reversible coordination is achieved by repositioning the heme more deeply into a large internal cavity, the "heme sliding mechanism". Combining high pressure crystallography and coarse-grain simulations on wild type Ngb as well as two mutants, one (V101F) with unaffected and another (F106W) with decreased affinity for CO, we show that Ngb hinges around a rigid mechanical nucleus of five hydrophobic residues (V68, I72, V109, L113, Y137) during its conformational transition induced by gaseous ligand, that the intrinsic flexibility of the F-G loop appears essential to drive the heme sliding mechanism, and that residue Val 101 may act as a sensor of the interaction disruption between the heme and the distal histidine.