Structure and mechanism of energy-coupling factor transporters

Zhang, Peng

doi:10.1016/j.tim.2013.09.009

Cited by 33 publications

(43 citation statements)

References 36 publications

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“…X-ray crystal structures of folate and hydroxymethyl pyrimidine transporters reveal that the EcfS component sits on the L-shaped cleft of the EcfT (Figure 4) [27,39]. This is different from the side-by-side conformation found in the classical ABC transporters [31,32]. No significant contacts are observed between the EcfS and ATPase components.…”

Section: Intersubunit Interactionsmentioning

confidence: 87%

“…Extensive biochemical, biophysical and structural data from studies on the ABC transporters have provided a great deal of insight into the structure and function of these proteins (reviewed [31,32]). In contrast the ECF transporters, which have been identified relatively recently, have not been as well characterised [27,33].…”

Section: Molecular Organisationmentioning

confidence: 99%

“…Both contain a binding protein for capturing substrate, a means for coupling ATP hydrolysis to substrate translocation, and a pathway for transferring substrates across the lipid bilayer [19]. In the well-characterised (classical or canonical) ABC transporters these entities are represented by four or more individual subunits encoded by separate genes [31,32]. The core components consist of a pair of hydrophobic trans-membrane domains (TMDs) that create the trans-membrane tunnel and two soluble ATPase subunits that couple the hydrolysis of ATP to the transport of solutes [18].…”

Section: Molecular Organisationmentioning

confidence: 99%

“…In the nucleotide-free state the Walker A and LSGGQ motifs are separated, but come together in a closed conformation in the nucleotide bound state [44]. Many ATPases of bacterial ABC exporters function as homodimers, but most of the eukaryotic equivalents are heterodimers consisting of either one or two active ATPases [31,32]. Whilst one of the NBD subunits is devoid of a consensus sequence crucial for catalysing ATP hydrolysis, it is still required for assembly into a functional ATPase dimer [52].…”

Section: Intersubunit Interactionsmentioning

confidence: 99%

“…This is to avoid potentially lethal substrate accumulation or loss due to unregulated trafficking [51]. Structural data indicate that ABC importers and exporters undergo conformational changes from an ATP-bound open (outward facing) structure to an ADP-bound closed (inward facing) state [31,32,52]. The SBPs use a ligand-induced "clamping" mechanism to uniquely capture appropriate solutes and bring them to the "entry gate" of the translocation pore [43].…”

Section: Mechanism Of Solute Transportmentioning

confidence: 99%

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Mechanisms of Biotin Transport

Polyak¹

2015

Biochem Anal Biochem

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Section: Intersubunit Interactionsmentioning

confidence: 87%

Section: Molecular Organisationmentioning

confidence: 99%

Section: Molecular Organisationmentioning

confidence: 99%

Section: Intersubunit Interactionsmentioning

confidence: 99%

Section: Mechanism Of Solute Transportmentioning

confidence: 99%

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Mechanisms of Biotin Transport

Polyak¹

2015

Biochem Anal Biochem

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Biotin-mediated growth and gene expression in Staphylococcus aureus is highly responsive to environmental biotin

Satiaputra

Eijkelkamp

McDevitt

et al. 2018

Appl Microbiol Biotechnol

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Biotin (Vitamin B7) is a critical enzyme co-factor in metabolic pathways important for bacterial survival. Biotin is obtained either from the environment or by de novo synthesis, with some bacteria capable of both. In certain species, the bifunctional protein BirA plays a key role in biotin homeostasis as it regulates expression of biotin biosynthetic enzymes in response to biotin demand and supply. Here, we compare the effect of biotin on the growth of two bacteria that possess a bifunctional BirA, namely Escherichia coli and Staphylococcus aureus. Unlike E. coli that could fulfill its biotin requirements through de novo synthesis, S. aureus showed improved growth rates in media supplemented with 10 nM biotin. S. aureus also accumulated more radiolabeled biotin from the media highlighting its ability to efficiently scavenge exogenous material. These data are consistent with S. aureus colonizing low biotin microhabitats. We also demonstrate that the S. aureus BirA protein is a transcriptional repressor of BioY, a subunit of the biotin transporter, and an operon containing yhfT and yhfS, the products of which have a putative role in fatty acid homeostasis. Increased expression of bioY is proposed to help cue S. aureus for efficient scavenging in low biotin environments.

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Transport of nickel and cobalt ions into bacterial cells by S components of ECF transporters

Kirsch

Eitinger

2014

Biometals

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Energy-coupling factor (ECF) transporters form a distinct group of ABC-type micronutrient importers in prokaryotes that do not contain extracytoplasmic, soluble substrate-binding proteins. Instead, they consist of a transmembrane substrate-specific S component that interacts with a module composed of a moderately conserved transmembrane (T) component and ABC ATPases. The majority of S components is considered to act as high-affinity binding proteins that strictly depend on their cognate T and ATPase units for transport activity. For a fraction of biotin-specific S units, however, transport activity was demonstrated in their solitary state. Here, we compared the activities of nickel- and cobalt-specific ECF transporters in the presence and absence of their T and ATPase units. Accumulation assays with radioactive metal ions showed that the truncated transporters led to approx. 25% of cell-bound radioactivity compared to the holotransporters. Activity of urease, an intracellular nickel-dependent enzyme, was used as a reporter and clearly indicated that the cell-bound radioactivity correlates with the cytoplasmic metal concentration. The results demonstrate that S units of metal transporters not only bind their substrates on the cell surface but mediate transport across the membrane, a finding of general importance on the way to understand the mechanism of ECF transporters.

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Structure and mechanism of energy-coupling factor transporters

Cited by 33 publications

References 36 publications

Mechanisms of Biotin Transport

Mechanisms of Biotin Transport

Biotin-mediated growth and gene expression in Staphylococcus aureus is highly responsive to environmental biotin

Transport of nickel and cobalt ions into bacterial cells by S components of ECF transporters

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