Role of PheE15 Gate in Ligand Entry and Nitric Oxide Detoxification Function of Mycobacterium tuberculosis Truncated Hemoglobin N

The truncated hemoglobin N, HbN, of Mycobacterium tuberculosis is endowed with a potent nitric oxide dioxygenase (NOD) activity that allows it to relieve nitrosative stress and enhance in vivo survival of its host. Despite its small size, the protein matrix of HbN hosts a two-branched tunnel, consis...

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Detalles Bibliográficos
Autores principales: Martí, Marcelo Adrián, Boechi, Leonardo, Estrin, Dario Ariel
Publicado: 2012
Materias:
alanine
dioxygenase
heme
isoleucine
nitric oxide dioxygenase
oxygen
phenylalanine
phenylalanine 15
truncated hemoglobin
truncated hemoglobin N
tryptophan
tyrosine
unclassified drug
article
conformational transition
controlled study
detoxification
down regulation
enzyme activity
ligand binding
molecular dynamics
mutant
mutational analysis
Mycobacterium tuberculosis
nonhuman
oxidation
oxygen affinity
site directed mutagenesis
structure analysis
wild type
Bacterial Proteins
Binding Sites
Carbon Monoxide
Computer Simulation
Crystallography, X-Ray
Ligands
Mutagenesis, Site-Directed
Nitric Oxide
Oxygen
Phenylalanine
Protein Structure, Tertiary
Truncated Hemoglobins
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v7_n11_p_Oliveira
http://hdl.handle.net/20.500.12110/paper_19326203_v7_n11_p_Oliveira
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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