[English] 日本語
Yorodumi
- PDB-8by2: Structure of the K+/H+ exchanger KefC with GSH. -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8by2
TitleStructure of the K+/H+ exchanger KefC with GSH.
ComponentsGlutathione-regulated potassium-efflux system protein KefC
KeywordsMEMBRANE PROTEIN / potassium proton exchanger / KefC / Transporter / CPA / GSH
Function / homology
Function and homology information


glutathione-regulated potassium exporter activity / response to methylglyoxal / antiporter activity / toxic substance binding / proton transmembrane transport / enzyme binding / plasma membrane
Similarity search - Function
Glutathione-regulated potassium-efflux system protein KefC / K+/H+ exchanger / Potassium uptake protein TrkA / Sodium/solute symporter superfamily / Cation/H+ exchanger / Sodium/hydrogen exchanger family / Regulator of K+ conductance, N-terminal / TrkA-N domain / RCK N-terminal domain profile. / NAD(P)-binding domain superfamily
Similarity search - Domain/homology
ADENOSINE MONOPHOSPHATE / GLUTATHIONE / : / Chem-PGW / Glutathione-regulated potassium-efflux system protein KefC
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.18 Å
AuthorsGulati, A. / Drew, D.
Funding supportEuropean Union, Sweden, 2items
OrganizationGrant numberCountry
European Research Council (ERC)ERC-CoG-820187European Union
Swedish Research Council Sweden
CitationJournal: To be published
Title: Structure and mechanism of the K+/H+ exchanger KefC
Authors: Gulati, A. / Drew, D.
History
DepositionDec 11, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 27, 2023Provider: repository / Type: Initial release
Revision 1.1Mar 27, 2024Group: Database references / Structure summary / Category: citation / struct / Item: _citation.journal_abbrev / _struct.title

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Glutathione-regulated potassium-efflux system protein KefC
B: Glutathione-regulated potassium-efflux system protein KefC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)125,25210
Polymers122,3662
Non-polymers2,8858
Water0
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14250 Å2
ΔGint-95 kcal/mol
Surface area47970 Å2
MethodPISA

-
Components

#1: Protein Glutathione-regulated potassium-efflux system protein KefC / K(+)/H(+) antiporter


Mass: 61183.223 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli)
Gene: kefC, kefC_3, kefC_4, A9X72_21045, ACU57_16285, AT845_001330, BHS81_26455, BJJ90_21970, BLM69_001595, BMT91_01970, BN17_44701, BON64_08355, BON68_06240, BON72_08730, BON76_14820, BON94_26490, ...Gene: kefC, kefC_3, kefC_4, A9X72_21045, ACU57_16285, AT845_001330, BHS81_26455, BJJ90_21970, BLM69_001595, BMT91_01970, BN17_44701, BON64_08355, BON68_06240, BON72_08730, BON76_14820, BON94_26490, BON97_15340, BRV02_001703, BTQ06_18350, BvCmsF30A_01124, BvCmsHHP056_04946, BvCmsKKP061_01751, BvCmsKSNP073_00849, BVL39_02825, C0P57_001700, C1Q91_003817, CCS08_23225, CIG67_13365, CR538_21280, CV83915_01528, CWS33_08975, D3Y67_20250, D9H94_05730, DAH19_13555, DAH22_04310, DAH27_12485, DAH28_04320, DAH29_14050, DAH30_11255, DAH32_09665, DAH37_05870, DAH41_08355, DEN89_19705, DEN90_18045, DEN96_05545, DEN97_05070, DEN98_05075, DEN99_02470, DEO00_04545, DEO12_14740, DEO14_11885, DEO19_04855, DIV22_05610, DRW19_05570, DS732_05130, DTL43_06565, DXT69_02135, DXT71_01260, E2121_11235, E2122_03850, E2127_05310, E2128_11280, E2129_03465, E2131_02880, E2132_05315, E2135_03750, E5P26_16110, E5P27_07520, E5P28_15370, E5P29_09025, E5P30_07860, E5P39_14645, E5P41_09555, E5P42_00460, E5P43_10360, E5P44_10710, E5P45_09675, E5P46_12140, E5P47_12165, E5P48_11095, E5P49_12390, E5P50_01615, E5P51_19605, E5S35_00760, E5S38_08180, E5S42_10720, E5S43_02390, E5S45_05455, E5S52_10125, E6D34_01595, EAI46_08450, EBP16_09705, EC95NR1_04226, EHD79_22595, EKI52_11150, EL79_3823, EL80_3769, ELT21_05100, ELV08_16095, ELY39_00725, ERS139208_01108, F0L67_09735, FDM60_06480, FJQ40_06620, FPJ29_04385, G3V95_03045, G4A38_11120, G4A47_11350, GAI66_03965, GF699_05360, GNZ05_10415, GOP25_07850, GP944_03730, GP965_24280, GQM04_06640, GRW24_15515, GUC01_17280, HNC36_14075, HV209_00940, J5U05_003215, JFD_01135, JNP96_04415, NCTC10865_05215, NCTC8960_01687, NCTC9036_04147, SAMEA3753106_01628, WR15_01725
Production host: Escherichia coli (E. coli) / References: UniProt: J7Q5Y6
#2: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: K / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-AMP / ADENOSINE MONOPHOSPHATE / Adenosine monophosphate


Mass: 347.221 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H14N5O7P / Feature type: SUBJECT OF INVESTIGATION / Comment: AMP*YM
#4: Chemical ChemComp-GSH / GLUTATHIONE / Glutathione


Mass: 307.323 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H17N3O6S / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical ChemComp-PGW / (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate / 1-Palmitoyl-2-Oleoyl-sn-Glycero-3-[Phospho-(1-glycerol)] / PHOSPHATIDYLGLYCEROL / Phosphatidylglycerol


Mass: 749.007 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C40H77O10P / Feature type: SUBJECT OF INVESTIGATION / Comment: phospholipid*YM
Has ligand of interestY

-
Experimental details

-
Experiment

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

-
Sample preparation

ComponentName: Kefc protein dimer with GSH / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Escherichia coli (E. coli)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 %

-
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 FIELDBright-field microscopy / Nominal magnification: 130000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 600 nm / C2 aperture diameter: 50 µm
Image recordingElectron dose: 64.3 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

-
Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.18 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 260115 / Symmetry type: POINT
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 82.62 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0028700
ELECTRON MICROSCOPYf_angle_d0.49411755
ELECTRON MICROSCOPYf_dihedral_angle_d9.831280
ELECTRON MICROSCOPYf_chiral_restr0.0341396
ELECTRON MICROSCOPYf_plane_restr0.0041459

+
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