Role of an orphan substrate-binding protein MhuP in transient heme transfer in Mycobacterium tuberculosis

Mandal, Suraj Kumar; Kanaujia, Shankar Prasad

doi:10.1016/j.ijbiomac.2022.05.059

Cited by 3 publications

(2 citation statements)

References 66 publications

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“…The failure to obtain the structure of heme-bound DppABCD may therefore be due to the interference by endogenous peptides, suggesting that heme and peptides could have partially overlapping binding pockets in Mtb DppA. In addition, it has been reported that the exogenous heme uptake mediated by DppABCD requires the assistance of another orphan SBP, Mhup, in Mtb ( 49 ). Thus, further studies are needed to elucidate how cluster C SBPs recognize and bind heme.…”

Section: Discussionmentioning

confidence: 99%

Molecular basis for substrate transport of Mycobacterium tuberculosis ABC importer DppABCD

Hu,

Yang,

Zhu

et al. 2024

Sci. Adv.

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The type I adenosine 5′-triphosphate (ATP)–binding cassette (ABC) transporter DppABCD is believed to be responsible for the import of exogenous heme as an iron source into the cytoplasm of the human pathogen Mycobacterium tuberculosis ( Mtb ). Additionally, this system is also known to be involved in the acquisition of tri- or tetra-peptides. Here, we report the cryo–electron microscopy structures of the dual-function Mtb DppABCD transporter in three forms, namely, the apo , substrate-bound, and ATP-bound states. The apo structure reveals an unexpected and previously uncharacterized assembly mode for ABC importers, where the lipoprotein DppA, a cluster C substrate-binding protein (SBP), stands upright on the translocator DppBCD primarily through its hinge region and N-lobe. These structural data, along with biochemical studies, reveal the assembly of DppABCD complex and the detailed mechanism of DppABCD-mediated transport. Together, these findings provide a molecular roadmap for understanding the transport mechanism of a cluster C SBP and its translocator.

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Section: Discussionmentioning

confidence: 99%

Molecular basis for substrate transport of Mycobacterium tuberculosis ABC importer DppABCD

Hu,

Yang,

Zhu

et al. 2024

Sci. Adv.

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“…Orphan MppA binds the murein tripeptide and functions with the core transporter OppBCDF in E. coli K12 [33]. An orphan heme‐bound protein MhuP in Mycobacterium tuberculosis binds and transports heme transiently to a peptide‐binding protein DppA belonging to the DppABCD transporter [34]. Although most of the bacterial orphan SBPs have not been specifically characterized, previous studies have shown that they have extensive and important roles.…”

Section: Discussionmentioning

confidence: 99%

A new l‐serine binding orphan SerBP affects indole synthesis in Pantoea ananatis

Zhang

Zheng

et al. 2023

J Basic Microbiol

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Indole is traditionally known as a metabolite of l‐tryptophan and now as an important signaling molecule in bacteria, however, the understanding of its upstream synthesis regulation is very limited. Pantoea ananatis YJ76, a predominant diazotrophic endophyte isolated from rice (Oryza sativa), can produce indole to regulate various physiological and biochemical behaviors. We constructed a mutant library of YJ76 using the mTn5 transposon insertion mutation method, from which an indole‐deficient mutant was screened out. Via high‐efficiency thermal asymmetric interlaced PCR (hiTAIL‐PCR), the transposon was determined to be inserted in a gene (RefSeq: WP014605468.1) of unknown function that is highly conserved at the intraspecific level. Bioinformatics analysis implied that the protein (Protein ID: WP089517194.1) encoded by the mutant gene is most likely to be a new orphan substrate‐binding protein (SBP) for amino acid ABC transporters. Amino acid supplement cultivation experiments and surface plasmon resonance revealed that the protein could bind to l‐serine (KD = 6.149 × 10−5 M). Therefore, the SBP was named as SerBP. This is the first case that a SBP responds to l‐serine ABC transports. As a precursor of indole synthesis, the transmembrane transported l‐serine was directly correlated with indole signal production and the mutation of serBP gene weakened the resistance of YJ76 to antibiotics, alkali, heavy metals, and starvation. This study provided a new paradigm for exploring the upstream regulatory pathway for indole synthesis of bacteria.

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An Update on Mycobacterium Tuberculosis Lipoproteins

Bigi,

Forrellad,

García

et al. 2023

Future Microbiol.

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Almost 3% of the proteins of Mycobacterium tuberculosis ( M. tuberculosis), the main causative agent of human tuberculosis, are lipoproteins. These lipoproteins are characteristic of the mycobacterial cell envelope and participate in many mechanisms involved in the pathogenesis of M. tuberculosis. In this review, the authors provide an updated analysis of M. tuberculosis lipoproteins and categorize them according to their demonstrated or predicted functions, including transport of compounds to and from the cytoplasm, biosynthesis of the mycobacterial cell envelope, defense and resistance mechanisms, enzymatic activities and signaling pathways. In addition, this updated analysis revealed that at least 40% of M. tuberculosis lipoproteins are glycosylated.

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Role of an orphan substrate-binding protein MhuP in transient heme transfer in Mycobacterium tuberculosis

Cited by 3 publications

References 66 publications

Molecular basis for substrate transport of Mycobacterium tuberculosis ABC importer DppABCD

Molecular basis for substrate transport of Mycobacterium tuberculosis ABC importer DppABCD

A new l‐serine binding orphan SerBP affects indole synthesis in Pantoea ananatis

An Update on Mycobacterium Tuberculosis Lipoproteins

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