+Open data
-Basic information
Entry | Database: PDB / ID: 6pan | ||||||
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Title | Structure of a bacterial Atm1-family ABC exporter with ATP bound | ||||||
Components | ATM1-type heavy metal exporter | ||||||
Keywords | TRANSPORT PROTEIN / ABC transporter / ABC exporter / ATPase / membrane protein | ||||||
Function / homology | Function and homology information Translocases / response to mercury ion / ABC-type transporter activity / monoatomic ion transport / ATP hydrolysis activity / ATP binding / plasma membrane Similarity search - Function | ||||||
Biological species | Novosphingobium aromaticivorans (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.4 Å | ||||||
Authors | Fan, C. / Kaiser, J.T. / Rees, D.C. | ||||||
Funding support | United States, 1items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2020 Title: A structural framework for unidirectional transport by a bacterial ABC exporter. Authors: Chengcheng Fan / Jens T Kaiser / Douglas C Rees / Abstract: The ATP-binding cassette (ABC) transporter of mitochondria (Atm1) mediates iron homeostasis in eukaryotes, while the prokaryotic homolog from (Atm1) can export glutathione derivatives and confer ...The ATP-binding cassette (ABC) transporter of mitochondria (Atm1) mediates iron homeostasis in eukaryotes, while the prokaryotic homolog from (Atm1) can export glutathione derivatives and confer protection against heavy-metal toxicity. To establish the structural framework underlying the Atm1 transport mechanism, we determined eight structures by X-ray crystallography and single-particle cryo-electron microscopy in distinct conformational states, stabilized by individual disulfide crosslinks and nucleotides. As Atm1 progresses through the transport cycle, conformational changes in transmembrane helix 6 (TM6) alter the glutathione-binding site and the associated substrate-binding cavity. Significantly, kinking of TM6 in the post-ATP hydrolysis state stabilized by MgADPVO eliminates this cavity, precluding uptake of glutathione derivatives. The presence of this cavity during the transition from the inward-facing to outward-facing conformational states, and its absence in the reverse direction, thereby provide an elegant and conceptually simple mechanism for enforcing the export directionality of transport by Atm1. One of the disulfide crosslinked Atm1 variants characterized in this work retains significant glutathione transport activity, suggesting that ATP hydrolysis and substrate transport by Atm1 may involve a limited set of conformational states with minimal separation of the nucleotide-binding domains in the inward-facing conformation. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6pan.cif.gz | 482.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6pan.ent.gz | 396.5 KB | Display | PDB format |
PDBx/mmJSON format | 6pan.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6pan_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 6pan_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 6pan_validation.xml.gz | 41 KB | Display | |
Data in CIF | 6pan_validation.cif.gz | 54.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pa/6pan ftp://data.pdbj.org/pub/pdb/validation_reports/pa/6pan | HTTPS FTP |
-Related structure data
Related structure data | 6pamC 6paoC 6paqC 6parC 6vqtC 6vquC 2hydS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
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-Assembly
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Noncrystallographic symmetry (NCS) | NCS domain:
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