4O1T

Crystal structure of murine neuroglobin mutant F106W

Summary for 4O1T

• Entry DOI: 10.2210/pdb4o1t/pdb
• Related: 1Q1F 4MU5 4NZI 4O2G 4O35
• Descriptor: Neuroglobin, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: globin, oxygen storage-transporter, transport protein
• Biological source: Mus musculus (mouse)
• Cellular location: Perikaryon (By similarity): Q9ER97
• Total number of polymer chains: 1
• Total formula weight: 18058.16

Authors

Avella, G.,Savino, C.,Vallone, B. (deposition date: 2013-12-16, release date: 2014-06-18, Last modification date: 2024-02-28)

Primary citation

Avella, G.,Ardiccioni, C.,Scaglione, A.,Moschetti, T.,Rondinelli, C.,Montemiglio, L.C.,Savino, C.,Giuffre, A.,Brunori, M.,Vallone, B.
Engineering the internal cavity of neuroglobin demonstrates the role of the haem-sliding mechanism.
Acta Crystallogr.,Sect.D, 70:1640-1648, 2014

PubMed 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.

PubMed: 24914975
DOI: 10.1107/S1399004714007032

Experimental method

X-RAY DIFFRACTION (1.6 Å)