Crystal structure of the ATP-binding subunit of an ABC transporter

Hung, Li‐Wei; Wang, Iris Xiaoyan; Nikaido, Kishiko; Liu, Peiqi; Ames, Giovanna Ferro‐Luzzi; Kim, Sung‐Hou

doi:10.1038/25393

Cited by 658 publications

(733 citation statements)

References 30 publications

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“…Therefore, TAPL can be energized by different nucleoside triphosphates with a slight predilection for purine based nucleotides. This broad specificity is also found with other ABC transporters (Alshawi and Senior 1993;Meyer et al 1994;Müller et al 1994) and results from only a π−π interaction between the base of the nucleotide with the NBD (Hung et al 1998). …”

Section: Nucleotide-dependent Peptide Transportsupporting

confidence: 67%

TAP and TAP-like — Brothers in arms?

Zhao

Tampé

Abele

2006

Naunyn Schmied Arch Pharmacol

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The transporter associated with antigen processing like (TAPL, ABCB9) is a member of the ATP-binding cassette (ABC) transporter family. Moreover, TAPL belongs to the TAP family due to its high sequence homology to TAP1 and TAP2. TAPL forms a homodimer which is localized in lysosomes with a minor fraction in the ER. It functions as an ATP-dependent peptide transporter which shows a broad peptide specificity ranging from 6-mer up to 59-mer peptides. In contrast to TAP, TAPL transports peptides with low affinity but high efficiency. This review will briefly summarize current knowledge about the structural organization and possible physiological function of TAPL in antigen processing and presentation.

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Section: Nucleotide-dependent Peptide Transportsupporting

confidence: 67%

TAP and TAP-like — Brothers in arms?

Zhao

Tampé

Abele

2006

Naunyn Schmied Arch Pharmacol

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“…The first high-resolution X-ray structure, of an isolated NBD from the Salmonella histidine transporter (HisP; [8]), has been followed by over a dozen NBD structures. All, not unexpectedly, have a very similar tertiary fold.…”

Section: Structure Of Abc Transportersmentioning

confidence: 99%

Structure and function of ABC transporters: the ATP switch provides flexible control

Linton

Higgins

2006

Pflugers Arch - Eur J Physiol

189

160

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ATP-binding cassette (ABC) transporters are ubiquitous integral membrane proteins that facilitate the transbilayer movement of ligands. They comprise, minimally, two transmembrane domains, which impart ligand specificity, and two nucleotide-binding domains (NBDs), which power the transport cycle. Almost 25 years of biochemistry is reviewed in light of the recent structure analyses resulting in the ATP-switch model for function in which the NBDs switch between a dimeric conformation, closed around two molecules of ATP, and a nucleotide-free, dimeric 'open' conformation. The flexibility of this switching mechanism has evolved to provide different kinetic control for different transporters and has also been co-opted to diverse functions other than transmembrane transport.

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“…In parallel with the analysis of RbsA, the groups of Kim and Ames determined the structure of the ABC-NBD HisP with bound ATP but no Mg 2+ (Hung et al 1998). In vivo, in complex with the membrane embedded domains HisQ and HisM, HisP constitutes the periplasmic histidine permease of Salmonella typhimurium, HisQMP 2 .…”

Section: Conformation Of the Monomermentioning

confidence: 99%

“…Here, the ATP molecules are facing away from each other and occupy a position, which is rather solvent exposed, leaving their 'backs' to make contacts. Thus, the HisP monomers are arranged in such way that the only intermolecular contacts are mediated by hydrophobic interactions between the antiparallel β-sheets of arm I of each monomer, explaining the 'nickname' of this particular formation (Hung et al 1998). The size of the dimer is around 60 Å × 40 Å × 90 Å.…”

Section: Dimeric Arrangement -Problems and Solutionsmentioning

confidence: 99%

The motor domains of ABC-transporters

Oswald

Holland

Schmitt

2006

Naunyn Schmied Arch Pharmacol

131

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The transport of substrates across a cellular membrane is a vitally important biological function essential for cell survival. ATP-binding cassette (ABC) transporters constitute one of the largest subfamilies of membrane proteins, accomplishing this task. Mutations in genes encoding for ABC transporters cause different diseases, for example, Adrenoleukodystrophy, Stargardt disease or Cystic Fibrosis. Furthermore, some ABC transporters are responsible for multidrug resistance, presenting a major obstacle in modern cancer chemotherapy. In order to translocate the enormous variety of substrates, ranging from ions, nutrients, small peptides to large toxins, different ABC-transporters utilize the energy gained from ATP binding and hydrolysis. The ATP binding cassette, also called the motor domain of ABC transporters, is highly conserved among all ABC transporters. The ability to purify this domain rather easily presents a perfect possibility to investigate the mechanism of ATP hydrolysis, thus providing us with a detailed picture of this process. Recently, many crystal structures of the ATP-binding domain and the full-length structures of two ABC transporters have been solved. Combining these structural data, we have now the opportunity to analyze the hydrolysis event on a molecular level. This review provides an overview of the structural investigations of the ATPbinding domains, highlighting molecular changes upon ATP binding and hydrolysis.

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Crystal structure of the ATP-binding subunit of an ABC transporter

Cited by 658 publications

References 30 publications

TAP and TAP-like — Brothers in arms?

TAP and TAP-like — Brothers in arms?

Structure and function of ABC transporters: the ATP switch provides flexible control

The motor domains of ABC-transporters

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