Diversity in ABC transporters: Type I, II and III importers

Rice, Austin J.; Park, Aekyung; Pinkett, Heather W.

doi:10.3109/10409238.2014.953626

Cited by 142 publications

(113 citation statements)

References 100 publications

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“…ABC importers are further divided into three categories; Type I, Type II and Type III transporters (also known as energy-coupling factor (ECF) transporters) [5]. This distinction evolved out of the differences in overall architecture and variations in the transport mechanism of each subtype.…”

Section: Introductionmentioning

confidence: 99%

“…Structural studies of ABC transporters in complex with SBPs have revealed how each SBP forms a complex with the TMDs of its cognate transporter to deliver substrate to the translocation pathway. Binding of substrate by the SBP and formation of the transporter complex determines selectivity for substrate transport (for comprehensive reviews on the mechanism and selectivity of ABC transporters see [5,11–13]). Alternatively, the S component of the ECF transporter binds substrate and rearranges position to deliver it across the lipid bilayer [14].…”

Section: Introductionmentioning

confidence: 99%

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Selective substrate uptake: The role of ATP-binding cassette (ABC) importers in pathogenesis

Tanaka

Song

Mason

et al. 2018

Biochimica et Biophysica Acta (BBA) - Biomembranes

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135

102

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The uptake of nutrients, including metals, amino acids and peptides are required for many biological processes. Pathogenic bacteria scavenge these essential nutrients from microenvironments to survive within the host. Pathogens must utilize a myriad of mechanisms to acquire these essential nutrients from the host while mediating the effects of toxicity. Bacteria utilize several transport proteins, including ATP-binding cassette (ABC) transporters to import and expel substrates. ABC transporters, conserved across all organisms, are powered by the energy from ATP to move substrates across cellular membranes. In this review, we will focus on nutrient uptake, the role of ABC importers at the host-pathogen interface, and explore emerging therapies to combat pathogenesis. This article is part of a Special Issue entitled: Beyond the Structure-Function Horizon of Membrane Proteins edited by Ute Hellmich, Rupak Doshi and Benjamin McIlwain.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Selective substrate uptake: The role of ATP-binding cassette (ABC) importers in pathogenesis

Tanaka

Song

Mason

et al. 2018

Biochimica et Biophysica Acta (BBA) - Biomembranes

Self Cite

135

102

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“…BCCT carriers are membrane proteins, most of which contain 12 predicted transmembrane ␣-helices (14,15). ABC transporters are one of the oldest and largest protein superfamilies and are ubiquitous from prokaryotes to eukaryotes (16)(17)(18). In bacteria, ABC transporters are primarily responsible for cellular uptake of nutrients and the export of harmful substances (19).…”

mentioning

confidence: 99%

Mechanistic Insight into Trimethylamine N -Oxide Recognition by the Marine Bacterium Ruegeria pomeroyi DSS-3

Chen

Shao

et al. 2015

J Bacteriol

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Trimethylamine N-oxide (TMAO) is an important nitrogen source for marine bacteria. TMAO can also be metabolized by marine bacteria into volatile methylated amines, the precursors of the greenhouse gas nitrous oxide. However, it was not known how TMAO is recognized and imported by bacteria. Ruegeria pomeroyi DSS-3, a marine Roseobacter, has an ATP-binding cassette transporter, TmoXWV, specific for TMAO. TmoX is the substrate-binding protein of the TmoXWV transporter. In this study, the substrate specificity of TmoX of R. pomeroyi DSS-3 was characterized. We further determined the structure of the TmoX/TMAO complex and studied the TMAO-binding mechanism of TmoX by biochemical, structural, and mutational analyses. A Ca 2؉ ion chelated by an extended loop in TmoX was shown to be important for maintaining the stability of TmoX. Molecular dynamics simulations indicate that TmoX can alternate between "open" and "closed" states for binding TMAO. In the substrate-binding pocket, four tryptophan residues interact with the quaternary amine of TMAO by cation-interactions, and Glu131 forms a hydrogen bond with the polar oxygen atom of TMAO. The -stacking interactions between the side chains of Phe and Trp are also essential for TMAO binding. Sequence analysis suggests that the TMAO-binding mechanism of TmoX may have universal significance in marine bacteria, especially in the marine Roseobacter clade. This study sheds light on how marine microorganisms utilize TMAO. IMPORTANCETrimethylamine N-oxide (TMAO) is an important nitrogen source for marine bacteria. The products of TMAO metabolized by bacteria are part of the precursors of the greenhouse gas nitrous oxide. It is unclear how TMAO is recognized and imported by bacteria. TmoX is the substrate-binding protein of a TMAO-specific transporter. Here, the substrate specificity of TmoX of Ruegeria pomeroyi DSS-3 was characterized. The TMAO-binding mechanism of TmoX was studied by biochemical, structural, and mutational analyses. Moreover, our results suggest that the TMAO-binding mechanism may have universal significance in marine bacteria. This study sheds light on how marine microorganisms utilize TMAO and should lead to a better understanding of marine nitrogen cycling.

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“…Indeed, the structural basis of binding protein interactions has recently been demonstrated for the ECF (energy-coupling factor) transporters, a distant branch of ABC importers with multiple binding protein partners per transporter (77). These studies may provide the framework for understanding the specificity of protein interactions in type I and type II ABC importers and provide additional insight into the diverse means by which ATP is utilized for transport (78). In conclusion, we propose that, as additional ABC importers are characterized, a spectrum of traits rather than discrete combinations will be the hallmark of this protein superfamily.…”

Section: Discussionmentioning

confidence: 99%

In Vitro Reassembly of the Ribose ATP-binding Cassette Transporter Reveals a Distinct Set of Transport Complexes

Clifton

Simon

Erramilli

et al. 2015

Journal of Biological Chemistry

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Background:The ribose transporter is a bacterial ABC importer with a non-canonical organization. Results: The binding protein complexes with the membrane domain in the absence of substrate, and the ATPase dissociates from the membrane domain during transport. Conclusion: A distinct model for transport is proposed from in vitro reassembly conditions and EPR data. Significance: The ribose transporter typifies the diversity of ABC transporter mechanisms.

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Diversity in ABC transporters: Type I, II and III importers

Cited by 142 publications

References 100 publications

Selective substrate uptake: The role of ATP-binding cassette (ABC) importers in pathogenesis

Selective substrate uptake: The role of ATP-binding cassette (ABC) importers in pathogenesis

Mechanistic Insight into Trimethylamine N -Oxide Recognition by the Marine Bacterium Ruegeria pomeroyi DSS-3

In Vitro Reassembly of the Ribose ATP-binding Cassette Transporter Reveals a Distinct Set of Transport Complexes

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