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dc.contributor.author
Lama, Amriti
dc.contributor.author
Pawarta, Sudesh
dc.contributor.author
Bidon Chanal, Axel
dc.contributor.author
Anand, Arvind
dc.contributor.author
Gelpi, José Luis
dc.contributor.author
Arya, Swati
dc.contributor.author
Marti, Marcelo Adrian
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dc.contributor.author
Estrin, Dario Ariel
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dc.contributor.author
Luque, F. Javier
dc.contributor.author
Dikshit, Kanak
dc.date.available
2019-05-06T00:09:50Z
dc.date.issued
2009
dc.identifier.citation
Lama, Amriti; Pawarta, Sudesh; Bidon Chanal, Axel; Anand, Arvind; Gelpi, José Luis; et al.; Role of the pre-A motif in nitric oxide scavenging by truncated hemoglobin HbN of Mycobacterium Tuberculosis; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 284; 2009; 14457-14468
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/75572
dc.description.abstract
Mycobacterium tuberculosis truncated hemoglobin, HbN, is endowed with a potent nitric-oxide dioxygenase activity and has been found to relieve nitrosative stress and enhance in vivo survival of a heterologous host, Salmonella enterica Typhimurium, within the macrophages. These findings implicate involvement of HbN in the defense of M. tuberculosis against nitrosative stress. The protein carries a tunnel system composed of a short and a long tunnel branch that has been proposed to facilitate diatomic ligand migration to the heme and an unusual Pre-A motif at the N terminus, which does not contribute significantly to the structural integrity of the protein, as it protrudes out of the compact globin fold. Strikingly, deletion of Pre-A region from the M. tuberculosis HbN drastically reduces its ability to scavenge nitric oxide (NO), whereas its insertion at the N terminus of Pre-A lacking HbN of Mycobacterium smegmatis improved its nitric-oxide dioxygenase activity. Titration of the oxygenated adduct of HbN and its mutants with NO indicated that the stoichiometric oxidation of protein is severalfold slower when the Pre-A region is deleted in HbN. Molecular dynamics simulations show that the excision of Pre-A motif results in distinct changes in the protein dynamics, which cause the gate of the tunnel long branch to be trapped into a closed conformation, thus impeding migration of diatomic ligands toward the heme active site. The present study, thus, unequivocally demonstrates vital function of Pre-A region in NO scavenging and unravels its unique role by which HbN might attain its efficient NO-detoxification ability.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Truncated Hemoglobin
dc.subject
Molecular Dynamics
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Role of the pre-A motif in nitric oxide scavenging by truncated hemoglobin HbN of Mycobacterium Tuberculosis
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-03-21T16:12:57Z
dc.journal.volume
284
dc.journal.pagination
14457-14468
dc.journal.pais
Estados Unidos
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dc.description.fil
Fil: Lama, Amriti. Council of Scientific and Industrial Research; India
dc.description.fil
Fil: Pawarta, Sudesh. Council of Scientific and Industrial Research; India
dc.description.fil
Fil: Bidon Chanal, Axel. Universitat de Barcelona; España
dc.description.fil
Fil: Anand, Arvind. Council of Scientific and Industrial Research; India
dc.description.fil
Fil: Gelpi, José Luis. Universitat de Barcelona; España
dc.description.fil
Fil: Arya, Swati. Council of Scientific and Industrial Research; India
dc.description.fil
Fil: Marti, Marcelo Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
dc.description.fil
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
dc.description.fil
Fil: Luque, F. Javier. Universitat de Barcelona; España
dc.description.fil
Fil: Dikshit, Kanak. Council of Scientific and Industrial Research; India
dc.journal.title
Journal of Biological Chemistry (online)
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/284/21/14457.long
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M807436200
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/pmid/19329431
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