5EU2

Crystal structure of murine neuroglobin mutant V101F at ambient pressure

Summary for 5EU2

• Entry DOI: 10.2210/pdb5eu2/pdb
• Related: 5EET
• Descriptor: Neuroglobin, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: globin, oxygen storage-transporter, transport protein, hpmx
• Biological source: Mus musculus (Mouse)
• Cellular location: Perikaryon : Q9ER97
• Total number of polymer chains: 1
• Total formula weight: 17395.46

Authors

Colloc'h, N.,Girard, E.,Vallone, B.,Prange, T. (deposition date: 2015-11-18, release date: 2016-10-19, Last modification date: 2024-01-10)

Primary citation

Colloc'h, N.,Sacquin-Mora, S.,Avella, G.,Dhaussy, A.C.,Prange, T.,Vallone, B.,Girard, E.
Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography.
Sci Rep, 7:1858-1858, 2017

PubMed 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.

PubMed: 28500341
DOI: 10.1038/s41598-017-02097-1

Experimental method

X-RAY DIFFRACTION (2 Å)