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- EMDB-40710: Cleaved Ycf1p Monomer in the IFwide-alpha conformation -

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Basic information

Entry
Database: EMDB / ID: EMD-40710
TitleCleaved Ycf1p Monomer in the IFwide-alpha conformation
Map dataCleaved Ycf1p Monomer in the IFwide-alpha conformation
Sample
  • Complex: Cleaved Ycf1p IFwide-alpha monomer
    • Protein or peptide: Metal resistance protein YCF1
    • Protein or peptide: Unknown peptide from Ycf1p R region
  • Ligand: (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate
KeywordsABC transporter / TRANSPORT PROTEIN
Function / homology
Function and homology information


ABC-type Cd2+ transporter / ABC-type cadmium transporter activity / Recycling of bile acids and salts / Heme degradation / Cytoprotection by HMOX1 / Aspirin ADME / Atorvastatin ADME / Transport of RCbl within the body / Paracetamol ADME / Synthesis of Leukotrienes (LT) and Eoxins (EX) ...ABC-type Cd2+ transporter / ABC-type cadmium transporter activity / Recycling of bile acids and salts / Heme degradation / Cytoprotection by HMOX1 / Aspirin ADME / Atorvastatin ADME / Transport of RCbl within the body / Paracetamol ADME / Synthesis of Leukotrienes (LT) and Eoxins (EX) / P-type cadmium transporter activity / Sphingolipid de novo biosynthesis / ABC-family protein mediated transport / vacuole fusion, non-autophagic / ABC-type glutathione-S-conjugate transporter / ABC-type glutathione S-conjugate transporter activity / fungal-type vacuole membrane / response to metal ion / response to cadmium ion / ABC-type transporter activity / cell redox homeostasis / glutathione metabolic process / transmembrane transport / membrane raft / ATP hydrolysis activity / ATP binding
Similarity search - Function
: / ABC transporter TMD0 domain / : / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter ...: / ABC transporter TMD0 domain / : / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Metal resistance protein YCF1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsBickers SC / Benlekbir S / Rubinstein JL / Kanelis V
Funding support Canada, 1 items
OrganizationGrant numberCountry
Natural Sciences and Engineering Research Council (NSERC, Canada)RGPIN-2020-05835 Canada
CitationJournal: Nat Commun / Year: 2024
Title: Structure of a dimeric full-length ABC transporter.
Authors: Sarah C Bickers / Samir Benlekbir / John L Rubinstein / Voula Kanelis /
Abstract: Activities of ATP binding cassette (ABC) proteins are regulated by multiple mechanisms, including protein interactions, phosphorylation, proteolytic processing, and/or oligomerization of the ABC ...Activities of ATP binding cassette (ABC) proteins are regulated by multiple mechanisms, including protein interactions, phosphorylation, proteolytic processing, and/or oligomerization of the ABC protein itself. Here we present the structure of yeast cadmium factor 1 (Ycf1p) in its mature form following cleavage by Pep4p protease. Ycf1p, a C subfamily ABC protein (ABCC), is homologue of human multidrug resistance protein 1. Remarkably, a portion of cleaved Ycf1p forms a well-ordered dimer, alongside monomeric particles also present in solution. While numerous other ABC proteins have been proposed to dimerize, no high-resolution structures have been reported. Both phosphorylation of the regulatory (R) region and ATPase activity are lower in the Ycf1p dimer compared to the monomer, indicating that dimerization affects Ycf1p function. The interface between Ycf1p protomers features protein-protein interactions and contains bound lipids, suggesting that lipids stabilize the dimer. The Ycf1p dimer structure may inform the dimerization interfaces of other ABCC dimers.
History
DepositionMay 4, 2023-
Header (metadata) releaseMay 8, 2024-
Map releaseMay 8, 2024-
UpdateNov 27, 2024-
Current statusNov 27, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_40710.png

Downloads & links

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Map

FileDownload / File: emd_40710.map.gz / Format: CCP4 / Size: 163.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCleaved Ycf1p Monomer in the IFwide-alpha conformation
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.03 Å/pix.
x 350 pix.
= 360.5 Å		1.03 Å/pix.
x 350 pix.
= 360.5 Å		1.03 Å/pix.
x 350 pix.
= 360.5 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.03 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.92
Minimum - Maximum-3.7370608 - 5.9143667
Average (Standard dev.)-0.00033601376 (±0.1006575)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions350350350
Spacing350350350
CellA=B=C: 360.5 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half Map 1

Fileemd_40710_half_map_1.map
AnnotationHalf Map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half Map 2

Fileemd_40710_half_map_2.map
AnnotationHalf Map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Cleaved Ycf1p IFwide-alpha monomer

EntireName: Cleaved Ycf1p IFwide-alpha monomer
Components
  • Complex: Cleaved Ycf1p IFwide-alpha monomer
    • Protein or peptide: Metal resistance protein YCF1
    • Protein or peptide: Unknown peptide from Ycf1p R region
  • Ligand: (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate

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Supramolecule #1: Cleaved Ycf1p IFwide-alpha monomer

SupramoleculeName: Cleaved Ycf1p IFwide-alpha monomer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2

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Macromolecule #1: Metal resistance protein YCF1

MacromoleculeName: Metal resistance protein YCF1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: ABC-type Cd2+ transporter
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 174.024141 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAGNLVSWAC KLCRSPEGFG PISFYGDFTQ CFIDGVILNL SAIFMITFGI RDLVNLCKKK HSGIKYRRNW IIVSRMALVL LEIAFVSLA SLNISKEEAE NFTIVSQYAS TMLSLFVALA LHWIEYDRSV VANTVLLFYW LFETFGNFAK LINILIRHTY E GIWYSGQT ...String:
MAGNLVSWAC KLCRSPEGFG PISFYGDFTQ CFIDGVILNL SAIFMITFGI RDLVNLCKKK HSGIKYRRNW IIVSRMALVL LEIAFVSLA SLNISKEEAE NFTIVSQYAS TMLSLFVALA LHWIEYDRSV VANTVLLFYW LFETFGNFAK LINILIRHTY E GIWYSGQT GFILTLFQVI TCASILLLEA LPKKPLMPHQ HIHQTLTRRK PNPYDSANIF SRITFSWMSG LMKTGYEKYL VE ADLYKLP RNFSSEELSQ KLEKNWENEL KQKSNPSLSW AICRTFGSKM LLAAFFKAIH DVLAFTQPQL LRILIKFVTD YNS ERQDDH SSLQGFENNH PQKLPIVRGF LIAFAMFLVG FTQTSVLHQY FLNVFNTGMY IKSALTALIY QKSLVLSNEA SGLS STGDI VNLMSVDVQK LQDLTQWLNL IWSGPFQIII CLYSLYKLLG NSMWVGVIIL VIMMPLNSFL MRIQKKLQKS QMKYK DERT RVISEILNNI KSLKLYAWEK PYREKLEEVR NNKELKNLTK LGCYMAVTSF QFNIVPFLVS CCTFAVFVYT EDRALT TDL VFPALTLFNL LSFPLMIIPM VLNSFIEASV SIGRLFTFFT NEELQPDSVQ RLPKVKNIGD VAINIGDDAT FLWQRKP EY KVALKNINFQ AKKGNLTCIV GKVGSGKTAL LSCMLGDLFR VKGFATVHGS VAYVSQVPWI MNGTVKENIL FGHRYDAE F YEKTIKACAL TIDLAILMDG DKTLVGEKGI SLSGGQKARL SLARAVYARA DTYLLDDPLA AVDEHVARHL IEHVLGPNG LLHTKTKVLA TNKVSALSIA DSIALLDNGE ITQQGTYDEI TKDADSPLWK LLNNYGKKNN GKSNEFGDSS ESSVRESSIP VEGELEQLQ KLNDLDFGNS DAISLRRASD ATLGSIDFGD DENIAKREHR EQGKVKWNIY LEYAKACNPK SVCVFILFIV I SMFLSVMG NVWLKHWSEV NSRYGSNPNA ARYLAIYFAL GIGSALATLI QTIVLWVFCT IHASKYLHNL MTNSVLRAPM TF FETTPIG RILNRFSNDI YKVDALLGRT FSQFFVNAVK VTFTITVICA TTWQFIFIII PLSVFYIYYQ QYYLRTSREL RRL DSITRS PIYSHFQETL GGLATVRGYS QQKRFSHINQ CRIDNNMSAF YPSINANRWL AYRLELIGSI IILGAATLSV FRLK QGTLT AGMVGLSLSY ALQITQTLNW IVRMTVEVET NIVSVERIKE YADLKSEAPL IVEGHRPPKE WPSQGDIKFN NYSTR YRPE LDLVLKHINI HIKPNEKVGI VGRTGAGKSS LTLALFRMIE ASEGNIVIDN IAINEIGLYD LRHKLSIIPQ DSQVFE GTV RENIDPINQY TDEAIWRALE LSHLKEHVLS MSNDGLDAQL TEGGGNLSVG QRQLLCLARA MLVPSKILVL DEATAAV DV ETDKVVQETI RTAFKDRTIL TIAHRLNTIM DSDRIIVLDN GKVAEFDSPG QLLSDNKSLF YSLCMEAGLV NENDYKDH D GDYKDHDIDY KDDDDK

UniProtKB: Metal resistance protein YCF1

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Macromolecule #2: Unknown peptide from Ycf1p R region

MacromoleculeName: Unknown peptide from Ycf1p R region / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 1.209482 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)

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Macromolecule #3: (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradeca...

MacromoleculeName: (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate
type: ligand / ID: 3 / Number of copies: 1 / Formula: 8PE
Molecular weightTheoretical: 691.959 Da
Chemical component information

ChemComp-8PE:
(2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate / phospholipid*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE / Instrument: LEICA EM GP

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 46.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 76300
Startup modelType of model: OTHER
Details: Cleaved Ycf1p Monomer in the IFwide-beta conformation
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 76300
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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