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primary topic: Role of Pre-A motif in nitric oxide scavenging by truncated hemoglobin, HbN, of Mycobacterium tuberculosis.

Role of Pre-A motif in nitric oxide scavenging by truncated hemoglobin, HbN, of Mycobacterium tuberculosis.
type: AcademicArticle
type: Article
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.
date: 2009-05-22
volume: 284
issue: 21
is part of: The Journal of biological chemistry
status: peerReviewed
status: published
author list: authors
type: EPrint
type: ArticleEPrint
is part of: repository
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subject: QD Chemistry

Role of Pre-A motif in nitric oxide scavenging by truncated hemoglobin, HbN, of Mycobacterium tuberculosis. (PDF)
type: Document
has file: dikshit09.pdf
has part: dikshit09.pdf

ASBMB
type: Organization

The Journal of biological chemistry
type: Collection
issn: 00219258

F Javier Luque
type: Person
given name: F Javier
family name: Luque

Sudesh Pawaria
type: Person
given name: Sudesh
family name: Pawaria

Kanak L Dikshit
type: Person
given name: Kanak L
family name: Dikshit

Marcelo Martí
type: Person
given name: Marcelo
family name: Martí

José Luis Gelpí
type: Person
given name: José Luis
family name: Gelpí

Axel Bidon-Chanal
type: Person
given name: Axel
family name: Bidon-Chanal

Arvind Anand
type: Person
given name: Arvind
family name: Anand

Swati Arya
type: Person
given name: Swati
family name: Arya

Dario A Estrin
type: Person
given name: Dario A
family name: Estrin

Amrita Lama
type: Person
given name: Amrita
family name: Lama

Role of Pre-A motif in nitric oxide scavenging by truncated hemoglobin, HbN, of Mycobacterium tuberculosis. (Image (PNG))
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Role of Pre-A motif in nitric oxide scavenging by truncated hemoglobin, HbN, of Mycobacterium tuberculosis. (Image (PNG))
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Role of Pre-A motif in nitric oxide scavenging by truncated hemoglobin, HbN, of Mycobacterium tuberculosis. (Indexer Terms)
type: Document
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primary topic: Role of Pre-A motif in nitric oxide scavenging by truncated hemoglobin, HbN, of Mycobacterium tuberculosis.

QD Chemistry
type: Concept