PDBsum entry 4o2g

Transport protein

PDB id: 4o2g

Contents

Protein chain

146 a.a.

Ligands

HEM-CMO

PDB id:

4o2g

Name:

Transport protein

Title:

Crystal structure of carbomonoxy murine neuroglobin mutant v140w

Structure:

Neuroglobin. Chain: a. Engineered: yes. Mutation: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: ngb. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.70Å R-factor: 0.214 R-free: 0.270

Authors:

G.Avella,C.Savino,B.Vallone

Key ref:

G.Avella et al. (2014). Engineering the internal cavity of neuroglobin demonstrates the role of the haem-sliding mechanism. Acta Crystallogr D Biol Crystallogr, 70, 1640-1648. PubMed id: 24914975 DOI: 10.1107/S1399004714007032

Date:

17-Dec-13 Release date: 18-Jun-14

Protein chain

Q9ER97  (NGB_MOUSE) -  Neuroglobin from Mus musculus

Seq: 151 a.a.

Struc: 146 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1107/S1399004714007032

Acta Crystallogr D Biol Crystallogr 70:1640-1648 (2014)

PubMed id: 24914975

Engineering the internal cavity of neuroglobin demonstrates the role of the haem-sliding mechanism.

G.Avella, C.Ardiccioni, A.Scaglione, T.Moschetti, C.Rondinelli, L.C.Montemiglio, C.Savino, A.Giuffrè, M.Brunori, B.Vallone.

ABSTRACT

Neuroglobin is a member of the globin family involved in neuroprotection; it is primarily expressed in the brain and retina of vertebrates. Neuroglobin belongs to the heterogeneous group of hexacoordinate globins that have evolved in animals, plants and bacteria, endowed with the capability of reversible intramolecular coordination, allowing the binding of small gaseous ligands (O2, NO and CO). In a unique fashion among haemoproteins, ligand-binding events in neuroglobin are dependent on the sliding of the haem itself within a preformed internal cavity, as revealed by the crystal structure of its CO-bound derivative. Point mutants of the neuroglobin internal cavity have been engineered and their functional and structural characterization shows that hindering the haem displacement leads to a decrease in CO affinity, whereas reducing the cavity volume without interfering with haem sliding has negligible functional effects.