[English] 日本語
Yorodumi
- EMDB-0873: Cryo-EM structure of Dnf1 from Chaetomium thermophilum in the E1-... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-0873
TitleCryo-EM structure of Dnf1 from Chaetomium thermophilum in the E1-ATP state
Map data
Sample
  • Complex: Heterodimer of Dnf1-Cdc50
    • Protein or peptide: Phospholipid-transporting ATPase
    • Protein or peptide: Cdc50
  • Ligand: MAGNESIUM ION
  • Ligand: PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
  • Ligand: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
Function / homology
Function and homology information


ATPase-coupled intramembrane lipid transporter activity / phospholipid transport / P-type phospholipid transporter / phospholipid translocation / magnesium ion binding / ATP hydrolysis activity / ATP binding / membrane
Similarity search - Function
Phospholipid-transporting P-type ATPase / CDC50/LEM3 family / LEM3 (ligand-effect modulator 3) family / CDC50 family / P-type ATPase, subfamily IV / P-type ATPase, C-terminal / P-type ATPase, N-terminal / Phospholipid-translocating ATPase N-terminal / Phospholipid-translocating P-type ATPase C-terminal / P-type ATPase, haloacid dehalogenase domain / P-type ATPase, phosphorylation site ...Phospholipid-transporting P-type ATPase / CDC50/LEM3 family / LEM3 (ligand-effect modulator 3) family / CDC50 family / P-type ATPase, subfamily IV / P-type ATPase, C-terminal / P-type ATPase, N-terminal / Phospholipid-translocating ATPase N-terminal / Phospholipid-translocating P-type ATPase C-terminal / 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
Phospholipid-transporting ATPase / Lem3/Cdc50
Similarity search - Component
Biological speciesChaetomium thermophilum var. thermophilum DSM 1495 (fungus) / Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsHe Y / Xu J / Wu X / Li L
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China31870835 China
CitationJournal: Protein Cell / Year: 2020
Title: Structures of a P4-ATPase lipid flippase in lipid bilayers.
Authors: Yilin He / Jinkun Xu / Xiaofei Wu / Long Li /
History
DepositionNov 19, 2019-
Header (metadata) releaseApr 29, 2020-
Map releaseApr 29, 2020-
UpdateJul 29, 2020-
Current statusJul 29, 2020Processing site: PDBj / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.02
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by height
  • Surface level: 0.02
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-6lcr
  • Surface level: 0.02
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_0873.map.gz / Format: CCP4 / Size: 87.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.055 Å
Density
Contour LevelBy AUTHOR: 0.02 / Movie #1: 0.02
Minimum - Maximum-0.1073686 - 0.18286814
Average (Standard dev.)0.00015012582 (±0.0030677575)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions284284284
Spacing284284284
CellA=B=C: 299.62 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0551.0551.055
M x/y/z284284284
origin x/y/z0.0000.0000.000
length x/y/z299.620299.620299.620
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS284284284
D min/max/mean-0.1070.1830.000

-
Supplemental data

-
Sample components

-
Entire : Heterodimer of Dnf1-Cdc50

EntireName: Heterodimer of Dnf1-Cdc50
Components
  • Complex: Heterodimer of Dnf1-Cdc50
    • Protein or peptide: Phospholipid-transporting ATPase
    • Protein or peptide: Cdc50
  • Ligand: MAGNESIUM ION
  • Ligand: PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
  • Ligand: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose

-
Supramolecule #1: Heterodimer of Dnf1-Cdc50

SupramoleculeName: Heterodimer of Dnf1-Cdc50 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Chaetomium thermophilum var. thermophilum DSM 1495 (fungus)
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast) / Recombinant strain: BJ5465

-
Macromolecule #1: Phospholipid-transporting ATPase

MacromoleculeName: Phospholipid-transporting ATPase / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: P-type phospholipid transporter
Source (natural)Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus)
Strain: DSM 1495 / CBS 144.50 / IMI 039719
Molecular weightTheoretical: 175.379531 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MAPPQEEGGG NGTELSMQRS RWATRRLTVK SGARKRLSLM TRAQAKNSAT EKRQSGVTDD GSPAADGDQK EGSISSSNNG GSAPRKLYF NLPLPPELKD EEGHPIQQFP RNKIRTAKYT PLSFIPKNLW FQFHNIANIF FLFLVILVIF PIFGGVNPGL N SVPLIVII ...String:
MAPPQEEGGG NGTELSMQRS RWATRRLTVK SGARKRLSLM TRAQAKNSAT EKRQSGVTDD GSPAADGDQK EGSISSSNNG GSAPRKLYF NLPLPPELKD EEGHPIQQFP RNKIRTAKYT PLSFIPKNLW FQFHNIANIF FLFLVILVIF PIFGGVNPGL N SVPLIVII TVTAIKDAIE DYRRTILDIE LNNAPVHRLQ GWENVNVEKD NVSLWRRFKK ANSRFFGSIW HLIERLWKED AQ SMRQRFA SADPRMSIET RTAPWDPSHR RSVASHTEEI QMTPVPSPVP HDPDVPTVSS AIENEATLLQ NLKGDLINHE IPV SGKARF HKDAWKNLVV GDFVRIYNDD ELPADIIILA TSDPDGACYV ETKNLDGETN LKVRQALRCG RTLKHARDCE RAQF VIESE PPQPNLYKYN GAIRWKQRVP WDPHGEPREM SEPIGIDNLL LRGCHLRNTE WALGVVVFTG HDTKIMMNAG ITPSK RARI ARELNFNVIC NFGILLIMCL IAAIANGIAW GKTDASLAWF EYGSIGGTPA LTGFITFWAA VIVFQNLVPI SLYISL EIV RTLQAFFIYS DVGMYYEKID QPCIPKSWNI SDDVGQIEYI FSDKTGTLTQ NVMEFKKATI NGQPYGEAYT EAQAGMD RR RGINVEEEAK VIREEIAAAK VRAIRGLREL HDNPYLHDED MTFIAPDFVE DLAGKNGPEQ QQATEHFMLA LALCHTVV A EKQPGDPPKM IFKAQSPDEA ALVATARDMG FTVLGMSDGG INVNVMGKDM HFPVLSIIEF NSSRKRMSTI VRMPDGRIL LFCKGADSVI YSRLKKGEQA DMRRETAQHL EMFAVEGLRT LCIAERELSE EEYREWRREH DLAATALENR EEKLEEVADK IERDLTLLG GTAIEDRLQD GVPDTIALLA DAGIKLWVLT GDKVETAINI GFSCNLLNND MDLLRLQVNE SDASTEDDYL Q LAEEQLKT NLERFNMTGD DEELKRARKD HNAPSPTYAL VIDGFTLRWV LSDSLKQKFL LLCKQCKSVL CCRVSPAQKA AV VSMVKNG LDVMTLSIGD GANDVAMIQE ADVGVGIAGE EGRQAVMSSD FAIGQFRFLQ RLVLVHGRWS YRRLAETISN FFY KNMIWT WSIFWYQCYC NFDIAYIFEY TYILMFNLFF TSVPVILMGV LDQDVSDTVS LAVPQLYRRG IERKEWTQTK FWLY MIDGV YQSVMSFFIP FIFVVLTPTA AGNGLDVSER TRLGAYIAHP AVITINGYIL INTYRWDWLM LLSIVLSDVF IFFWT GVYT ATTYSAGFYQ AAPQVYQELT FWMCLIVTPA LCLLPRLVVK CIQKQRFPYD VDIIREQANR GDFAAADAAA VAALGG PER VEGESLGSLS SSGKGSGRSK KSKHQQYASV DEDRRPIYPP SIATHNTRAQ NGSDGTTYIM QSRTSTELQQ EMPFDRD RE EETPAVRPSI ERTRPSYDRI RRSIDRVRPS FEASNDFTSA ARLSRIESTH SSLGHTYSHQ RESYAGESSG AQQGQEPG Q RRFNLATVRK RGLSAFSKKS IDTTEGEPPR EPPM

-
Macromolecule #2: Cdc50

MacromoleculeName: Cdc50 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus)
Strain: DSM 1495 / CBS 144.50 / IMI 039719
Molecular weightTheoretical: 46.452312 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MAPRRRRGAG QDGSDDGRSD SDAPKNRPPN TAFRQQRMRA WQCVLTPKLI VTVFSILAAI YLGFGAWLTY LAHTVRDLKI DYTDCLTSA PKDDFETIPQ NHITAHFSAK DSTFDPYKAQ WKTTEREVQV ANYTDNRQFC IVRFNIPEDL QPTISFFYYL E NFYQNHRR ...String:
MAPRRRRGAG QDGSDDGRSD SDAPKNRPPN TAFRQQRMRA WQCVLTPKLI VTVFSILAAI YLGFGAWLTY LAHTVRDLKI DYTDCLTSA PKDDFETIPQ NHITAHFSAK DSTFDPYKAQ WKTTEREVQV ANYTDNRQFC IVRFNIPEDL QPTISFFYYL E NFYQNHRR YVNSFNAKQL LGDAVDGKTI NDSTCDPITH DPKGTGKIVY PCGLVANSIF NDTFSSPLAL AVRNSSDSSR PY NMTTKGI AWPGLKDLYG KTSYSLDQIV PPPNWERRYK YGYQENNPPP DLKTDELFQN WMMLAAAPNF YKLYQKNDTH PML AGQYEI EIESNFDVTV YKGRKAFVIT TLSTMGSRNI WPGIIFLIVG GICLVLDIYF ILSFFIWRPR KLGDPSYLSW NQPS APGGH SS

-
Macromolecule #5: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 5 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

-
Macromolecule #6: PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER

MacromoleculeName: PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / type: ligand / ID: 6 / Number of copies: 1 / Formula: ACP
Molecular weightTheoretical: 505.208 Da
Chemical component information

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

-
Macromolecule #7: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phospho...

MacromoleculeName: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine
type: ligand / ID: 7 / Number of copies: 1 / Formula: P5S
Molecular weightTheoretical: 792.075 Da
Chemical component information

ChemComp-P5S:
O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine / Phosphatidylserine

-
Macromolecule #8: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 8 / Number of copies: 1 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration1.5 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 297 K / Instrument: FEI VITROBOT MARK IV

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Sample stageCooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 57.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Particle selectionNumber selected: 2397258
CTF correctionSoftware - Name: Gctf
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final 3D classificationNumber classes: 8 / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final reconstructionNumber classes used: 2 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 272912

-
Atomic model buiding 1

RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-6lcr:
Cryo-EM structure of Dnf1 from Chaetomium thermophilum in the E1-ATP state

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more