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- PDB-7nxf: Structure of the fungal plasma membrane proton pump Pma1 in its a... -

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Basic information

Entry
Database: PDB / ID: 7nxf
TitleStructure of the fungal plasma membrane proton pump Pma1 in its auto-inhibited state - monomer unit
ComponentsPlasma membrane ATPase
KeywordsPROTON TRANSPORT / Membrane Protein / P-Type ATPase / proton-transporting ATPase
Function / homology
Function and homology information


P-type H+-exporting transporter / proton export across plasma membrane / P-type proton-exporting transporter activity / ATP hydrolysis activity / ATP binding / plasma membrane
Similarity search - Function
P-type ATPase, subfamily IIIA / Cation transporter/ATPase, N-terminus / Cation-transporting P-type ATPase, N-terminal / Cation transporter/ATPase, N-terminus / P-type ATPase, haloacid dehalogenase domain / P-type ATPase, phosphorylation site / P-type ATPase, cytoplasmic domain N / E1-E2 ATPases phosphorylation site. / P-type ATPase, A domain superfamily / P-type ATPase ...P-type ATPase, subfamily IIIA / Cation transporter/ATPase, N-terminus / Cation-transporting P-type ATPase, N-terminal / Cation transporter/ATPase, N-terminus / P-type ATPase, haloacid dehalogenase domain / P-type ATPase, phosphorylation site / P-type ATPase, cytoplasmic domain N / E1-E2 ATPases phosphorylation site. / P-type ATPase, A domain superfamily / P-type ATPase / P-type ATPase, transmembrane domain superfamily / HAD superfamily / HAD-like superfamily
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / : / Plasma membrane ATPase
Similarity search - Component
Biological speciesNeurospora crassa (fungus)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsHeit, S. / Geurts, M.M.G. / Murphy, B.J. / Corey, R. / Mills, D.J. / Kuehlbrandt, W. / Bublitz, M.
Funding support United Kingdom, 5items
OrganizationGrant numberCountry
Other privateThe Academy of Medical Sciences United Kingdom
Other privateFEBS United Kingdom
Other privateEPA Cephalosporin Fund (CF 346) United Kingdom
Other privateErasmus+ United Kingdom
Other privateBiochemical Society United Kingdom
CitationJournal: Sci Adv / Year: 2021
Title: Structure of the hexameric fungal plasma membrane proton pump in its autoinhibited state.
Authors: Sabine Heit / Maxwell M G Geurts / Bonnie J Murphy / Robin A Corey / Deryck J Mills / Werner Kühlbrandt / Maike Bublitz /
Abstract: The fungal plasma membrane H-ATPase Pma1 is a vital enzyme, generating a proton-motive force that drives the import of essential nutrients. Autoinhibited Pma1 hexamers in the plasma membrane of ...The fungal plasma membrane H-ATPase Pma1 is a vital enzyme, generating a proton-motive force that drives the import of essential nutrients. Autoinhibited Pma1 hexamers in the plasma membrane of starving fungi are activated by glucose signaling and subsequent phosphorylation of the autoinhibitory domain. As related P-type adenosine triphosphatases (ATPases) are not known to oligomerize, the physiological relevance of Pma1 hexamers remained unknown. We have determined the structure of hexameric Pma1 from by electron cryo-microscopy at 3.3-Å resolution, elucidating the molecular basis for hexamer formation and autoinhibition and providing a basis for structure-based drug development. Coarse-grained molecular dynamics simulations in a lipid bilayer suggest lipid-mediated contacts between monomers and a substantial protein-induced membrane deformation that could act as a proton-attracting funnel.
History
DepositionMar 18, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 17, 2021Provider: repository / Type: Initial release
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Revision 1.1Dec 1, 2021Group: Database references / Category: citation / citation_author
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Assembly

Deposited unit
A: Plasma membrane ATPase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,4754
Polymers99,9841
Non-polymers4913
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration, native gel electrophoresis, microscopy, electron microscopy
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area1150 Å2
ΔGint-14 kcal/mol
Surface area38760 Å2

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Components

#1: Protein Plasma membrane ATPase


Mass: 99984.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Neurospora crassa (fungus)
References: UniProt: A0A0B0DXJ0, P-type H+-exporting transporter
#2: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
Has ligand of interestN
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Monomeric subunit of the hexameric fungal plasma membrane proton pump in its auto-inhibited state
Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: #1 / Source: NATURAL
Source (natural)Organism: Neurospora crassa (fungus) / Strain: FGSC #4761 / Cellular location: plasma membrane
Buffer solutionpH: 6.5
SpecimenConc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: C-flat-2/2
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 70 % / Chamber temperature: 283 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD
Image recordingElectron dose: 42 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

SoftwareName: PHENIX / Version: 1.18.2_3874: / Classification: refinement
EM software
IDNameVersionCategory
2EPUimage acquisition
9PHENIXmodel refinement
13RELION3.13D reconstruction
14PHENIX3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 293999 / Details: composite map of three 3D reconstructions / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0046530
ELECTRON MICROSCOPYf_angle_d0.6328871
ELECTRON MICROSCOPYf_dihedral_angle_d23.669887
ELECTRON MICROSCOPYf_chiral_restr0.0431037
ELECTRON MICROSCOPYf_plane_restr0.0051118

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