[English] 日本語
Yorodumi
- PDB-7y1b: 3.2 angstrom cryo-EM structure of extracellular region of mouse B... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7y1b
Title3.2 angstrom cryo-EM structure of extracellular region of mouse Basigin-2 in complex with the Fab fragment of antibody 6E7F1
Components
  • Heavy chain of 6E7F1
  • Isoform 2 of Basigin
  • Light chain of 6E7F1
KeywordsTRANSPORT PROTEIN / Transporter / glucose metabolism / monocarboxylic acid transport / alpha helical TMs
Function / homology
Function and homology information


Proton-coupled monocarboxylate transport / Aspirin ADME / Basigin interactions / acrosomal membrane / Degradation of the extracellular matrix / Integrin cell surface interactions / response to mercury ion / endothelial tube morphogenesis / neural retina development / photoreceptor cell maintenance ...Proton-coupled monocarboxylate transport / Aspirin ADME / Basigin interactions / acrosomal membrane / Degradation of the extracellular matrix / Integrin cell surface interactions / response to mercury ion / endothelial tube morphogenesis / neural retina development / photoreceptor cell maintenance / odontogenesis of dentin-containing tooth / D-mannose binding / decidualization / positive regulation of vascular endothelial growth factor production / photoreceptor outer segment / response to cAMP / neutrophil chemotaxis / embryo implantation / photoreceptor inner segment / positive regulation of endothelial cell migration / protein localization to plasma membrane / sarcolemma / response to peptide hormone / signaling receptor activity / spermatogenesis / basolateral plasma membrane / angiogenesis / cell differentiation / endoplasmic reticulum membrane / plasma membrane
Similarity search - Function
Immunoglobulin domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Biological speciesMus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.23 Å
AuthorsZhang, H. / Yang, X. / Xue, Y. / Huang, Y. / Mo, X. / Zhang, H. / Li, N. / Gao, N. / Li, X. / Wang, S. ...Zhang, H. / Yang, X. / Xue, Y. / Huang, Y. / Mo, X. / Zhang, H. / Li, N. / Gao, N. / Li, X. / Wang, S. / Gao, Y. / Liao, J.
Funding support China, 2items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2017YFA0504800 China
Ministry of Science and Technology (MoST, China)2018ZX09711003-003-003 China
CitationJournal: To Be Published
Title: Allosteric modulation of monocarboxylate transporters 1 and 4 by targeting their chaperon Basigin
Authors: Zhang, H. / Yang, X. / Xue, Y. / Huang, Y. / Mo, Y. / Zhang, H. / Li, N. / Gao, N. / Li, X. / Wang, S. / Gao, Y. / Liao, J.
History
DepositionJun 8, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 14, 2023Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / em_admin / pdbx_entry_details / pdbx_modification_feature
Item: _em_admin.last_update

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Isoform 2 of Basigin
H: Heavy chain of 6E7F1
L: Light chain of 6E7F1


Theoretical massNumber of molelcules
Total (without water)80,9083
Polymers80,9083
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, The combination of electron microscopy and biochemical assay indicate that the Basigin has extensive interactions with its antibody 6E7F1
TypeNameSymmetry operationNumber
identity operation1_5551

-
Components

#1: Protein Isoform 2 of Basigin / Basic immunoglobulin superfamily / HT7 antigen / Membrane glycoprotein gp42


Mass: 29707.447 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Bsg / Production host: Homo sapiens (human) / References: UniProt: P18572
#2: Antibody Heavy chain of 6E7F1


Mass: 25275.400 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse)
#3: Antibody Light chain of 6E7F1


Mass: 25924.785 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse)
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

ComponentName: 3.2 angstrom cryo-EM structure of extracellular region of mouse MCT1/Basigin-2 in complex with its monoclonal antibody 6E7F1
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 0.1 MDa / Experimental value: YES
Source (natural)Organism: Mus musculus (house mouse)
Source (recombinant)Organism: Homo sapiens (human) / Cell: HEK293S / Plasmid: pEG BacMam
Buffer solutionpH: 7.5 / Details: 20 mM HEPES pH7.5, 150 mM NaCl
Buffer component
IDConc.NameFormulaBuffer-ID
120 mMHEPES pH 7.5HEPES1
2150 mMNaClNaCl1
SpecimenConc.: 0.7 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: This sample is monodisperse
Specimen supportGrid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 283 K / Details: blot for 3.5-4.5 seconds before plunging

-
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: SPOT SCAN
Electron lensMode: DIFFRACTION / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm
Specimen holderCryogen: NITROGEN
Image recordingAverage exposure time: 2.5 sec. / Electron dose: 75 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 2842
Image scansSampling size: 1.9 µm / Width: 1034 / Height: 1034 / Movie frames/image: 48

-
Processing

EM software
IDNameVersionCategory
1cryoSPARC2.15particle selection
4cryoSPARC2.15CTF correction
7cryoSPARC2.15model fitting
9PHENIX1.19.2model refinement
10cryoSPARC2.15initial Euler assignment
11cryoSPARC2.15final Euler assignment
12cryoSPARC2.15classification
13cryoSPARC2.153D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 712923
3D reconstructionResolution: 3.23 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 106160 / Symmetry type: POINT
Atomic model buildingB value: 39.46 / Protocol: AB INITIO MODEL / Space: REAL / Target criteria: Correlation coefficient

+
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