[English] 日本語
Yorodumi
- EMDB-35643: Cryo-EM structure of heme transporter CydDC from Escherichia coli... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-35643
TitleCryo-EM structure of heme transporter CydDC from Escherichia coli in the occluded ATP bound state
Map data
Sample
  • Complex: CydDC
    • Protein or peptide: ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydC
    • Protein or peptide: ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydD
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
KeywordsABC transporter / Heme / TRANSPORT PROTEIN
Function / homology
Function and homology information


cysteine transport / glutathione transmembrane transport / ATPase-coupled lipid transmembrane transporter activity / ABC-type transporter activity / cell redox homeostasis / ATP hydrolysis activity / ATP binding / membrane
Similarity search - Function
ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydC / ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydD / Type 1 protein exporter / 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, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydC / ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydD / Type 1 protein exporter / 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
ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydC / ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydD
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsZhu C / Li J
Funding support China, 5 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2021YFA1300900 China
Ministry of Science and Technology (MoST, China)22ZR1441600 China
Other government22ZR1441600
Other governmentZD2021CY001
Other governmentLG202101-01-08 China
CitationJournal: Protein Cell / Year: 2023
Title: Cryo-EM structures of a prokaryotic heme transporter CydDC.
Authors: Chen Zhu / Yanfeng Shi / Jing Yu / Wenhao Zhao / Lingqiao Li / Jingxi Liang / Xiaolin Yang / Bing Zhang / Yao Zhao / Yan Gao / Xiaobo Chen / Xiuna Yang / Lu Zhang / Luke W Guddat / Lei Liu / ...Authors: Chen Zhu / Yanfeng Shi / Jing Yu / Wenhao Zhao / Lingqiao Li / Jingxi Liang / Xiaolin Yang / Bing Zhang / Yao Zhao / Yan Gao / Xiaobo Chen / Xiuna Yang / Lu Zhang / Luke W Guddat / Lei Liu / Haitao Yang / Zihe Rao / Jun Li /
History
DepositionMar 14, 2023-
Header (metadata) releaseJun 14, 2023-
Map releaseJun 14, 2023-
UpdateDec 13, 2023-
Current statusDec 13, 2023Processing site: PDBj / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_35643.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.96 Å/pix.
x 320 pix.
= 307.2 Å
0.96 Å/pix.
x 320 pix.
= 307.2 Å
0.96 Å/pix.
x 320 pix.
= 307.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.96 Å
Density
Contour LevelBy AUTHOR: 0.22
Minimum - Maximum-0.90131086 - 1.8307837
Average (Standard dev.)0.0033732967 (±0.056329962)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 307.19998 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: #2

Fileemd_35643_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_35643_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : CydDC

EntireName: CydDC
Components
  • Complex: CydDC
    • Protein or peptide: ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydC
    • Protein or peptide: ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydD
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE

-
Supramolecule #1: CydDC

SupramoleculeName: CydDC / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Escherichia coli (E. coli)

-
Macromolecule #1: ABC transporter, CydDC cysteine exporter (CydDC-E) family, permea...

MacromoleculeName: ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydC
type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 62.978914 KDa
Recombinant expressionOrganism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
SequenceString: MRALLPYLAL YKRHKWMLSL GIVLAIVTLL ASIGLLTLSG WFLSASAVAG VAGLYSFNYM LPAAGVRGAA ITRTAGRYFE RLVSHDATF RVLQHLRIYT FSKLLPLSPA GLARYRQGEL LNRVVADVDT LDHLYLRVIS PLVGAFVVIM VVTIGLSFLD F TLAFTLGG ...String:
MRALLPYLAL YKRHKWMLSL GIVLAIVTLL ASIGLLTLSG WFLSASAVAG VAGLYSFNYM LPAAGVRGAA ITRTAGRYFE RLVSHDATF RVLQHLRIYT FSKLLPLSPA GLARYRQGEL LNRVVADVDT LDHLYLRVIS PLVGAFVVIM VVTIGLSFLD F TLAFTLGG IMLLTLFLMP PLFYRAGKST GQNLTHLRGQ YRQQLTAWLQ GQAELTIFGA SDRYRTQLEN TEIQWLEAQR RQ SELTALS QAIMLLIGAL AVILMLWMAS GGVGGNAQPG ALIALFVFCA LAAFEALAPV TGAFQHLGQV IASAVRITDL TDQ KPEVTF PDTQTRVADR VSLTLRDVQF TYPEQSQQAL KGISLQVNAG EHIAILGRTG CGKSTLLQLL TRAWDPQQGE ILLN DSPIA SLNEAALRQT ISVVPQRVHL FSATLRDNLL LASPGSSDEA LSEILRRVGL EKLLEDAGLN SWLGEGGRQL SGGEL RRLA IARALLHDAP LVLLDQPTEG LDATTESQIL ELLAEMMREK TVLMVTHRLR GLSRFQQIIV MDNGQIIEQG THAELL ARQ GRYYQFKQGL

UniProtKB: ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydC

-
Macromolecule #2: ABC transporter, CydDC cysteine exporter (CydDC-E) family, permea...

MacromoleculeName: ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydD
type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli) / Strain: B / BL21-DE3
Molecular weightTheoretical: 65.143953 KDa
Recombinant expressionOrganism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
SequenceString: MNKSRQKELT RWLKQQSVIS QRWLNISRLL GFVSGILIIA QAWFMARILQ HMIMENIPRE ALLLPFTLLV LTFVLRAWVV WLRERVGYH AGQHIRFAIR RQVLDRLQQA GPAWIQGKPA GSWATLVLEQ IDDMHDYYAR YLPQMALAVS VPLLIVVAIF P SNWAAALI ...String:
MNKSRQKELT RWLKQQSVIS QRWLNISRLL GFVSGILIIA QAWFMARILQ HMIMENIPRE ALLLPFTLLV LTFVLRAWVV WLRERVGYH AGQHIRFAIR RQVLDRLQQA GPAWIQGKPA GSWATLVLEQ IDDMHDYYAR YLPQMALAVS VPLLIVVAIF P SNWAAALI LLGTAPLIPL FMALVGMGAA DANRRNFLAL ARLSGHFLDR LRGMETLRIF GRGEAEIESI RSASEDFRQR TM EVLRLAF LSSGILEFFT SLSIALVAVY FGFSYLGELD FGHYDTGVTL AAGFLALILA PEFFQPLRDL GTFYHAKAQA VGA ADSLKT FMETPLAHPQ RGEAELALTD PLTIEAEDLF ITSPEGKTLA GPLNFTLPAG QRAVLVGRSG SGKSSLLNAL SGFL SYQGS LRINGIELRD LSPESWRKHL SWVGQNPQLP AATLRDNVLL ARPDASEQEL QAALDNAWVS EFLPLLPQGV DTPVG DQAA RLSVGQAQRV AVARALLNPC SLLLLDQPAA SLDAHSEQRV MEALNAASLR QTTLMVTHQL EDLADWDVIW VMQDGR IIE QGRYAELSVA GGPFATLLAH RQEEI

UniProtKB: ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydD

-
Macromolecule #3: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 4 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 119296
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

+
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