 |
PDBsum entry 5eet
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transport protein
|
PDB id
|
|
|
|
5eet
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Determinants of neuroglobin plasticity highlighted by joint coarse-Grained simulations and high pressure crystallography.
|
|
|
Authors
|
|
N.Colloc'H,
S.Sacquin-Mora,
G.Avella,
A.C.Dhaussy,
T.Prangé,
B.Vallone,
E.Girard.
|
|
|
Ref.
|
|
Sci Rep, 2017,
7,
1858.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
