[English] 日本語
Yorodumi
- EMDB-11690: Human TRPV4 structure in presence of 4a-PDD -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-11690
TitleHuman TRPV4 structure in presence of 4a-PDD
Map data
Sample
  • Complex: Human TRPV4 in complex with 4a-PDD
    • Protein or peptide: Transient receptor potential cation channel subfamily V member 4,Green fluorescent protein
  • Ligand: CALCIUM ION
KeywordsIon channel. open-conformation / agonist / 4a-PDD / MEMBRANE PROTEIN
Function / homology
Function and homology information


stretch-activated, monoatomic cation-selective, calcium channel activity / blood vessel endothelial cell delamination / regulation of response to osmotic stress / osmosensor activity / vasopressin secretion / positive regulation of striated muscle contraction / calcium ion import into cytosol / negative regulation of brown fat cell differentiation / positive regulation of microtubule depolymerization / positive regulation of macrophage inflammatory protein 1 alpha production ...stretch-activated, monoatomic cation-selective, calcium channel activity / blood vessel endothelial cell delamination / regulation of response to osmotic stress / osmosensor activity / vasopressin secretion / positive regulation of striated muscle contraction / calcium ion import into cytosol / negative regulation of brown fat cell differentiation / positive regulation of microtubule depolymerization / positive regulation of macrophage inflammatory protein 1 alpha production / hyperosmotic salinity response / positive regulation of chemokine (C-X-C motif) ligand 1 production / positive regulation of chemokine (C-C motif) ligand 5 production / cartilage development involved in endochondral bone morphogenesis / cellular hypotonic salinity response / cortical microtubule organization / cellular hypotonic response / multicellular organismal-level water homeostasis / osmosensory signaling pathway / positive regulation of vascular permeability / positive regulation of monocyte chemotactic protein-1 production / cell-cell junction assembly / cell volume homeostasis / cellular response to osmotic stress / calcium ion import / regulation of aerobic respiration / TRP channels / cortical actin cytoskeleton / diet induced thermogenesis / positive regulation of macrophage chemotaxis / beta-tubulin binding / microtubule polymerization / calcium ion import across plasma membrane / alpha-tubulin binding / monoatomic cation channel activity / response to mechanical stimulus / cytoplasmic microtubule / SH2 domain binding / bioluminescence / protein kinase C binding / actin filament organization / generation of precursor metabolites and energy / filopodium / adherens junction / response to insulin / positive regulation of JNK cascade / calcium ion transmembrane transport / calcium channel activity / positive regulation of interleukin-6 production / ruffle membrane / intracellular calcium ion homeostasis / positive regulation of inflammatory response / calcium ion transport / actin filament binding / glucose homeostasis / lamellipodium / negative regulation of neuron projection development / actin binding / cellular response to heat / actin cytoskeleton organization / growth cone / positive regulation of cytosolic calcium ion concentration / microtubule binding / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / response to hypoxia / positive regulation of ERK1 and ERK2 cascade / calmodulin binding / cilium / apical plasma membrane / focal adhesion / lipid binding / protein kinase binding / negative regulation of transcription by RNA polymerase II / cell surface / endoplasmic reticulum / ATP binding / metal ion binding / identical protein binding / membrane / plasma membrane
Similarity search - Function
Transient receptor potential cation channel subfamily V member 4 / Transient receptor potential cation channel subfamily V member 1-4 / Transient receptor potential cation channel subfamily V / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Ankyrin repeat / Ankyrin repeat profile. / Ankyrin repeat region circular profile. ...Transient receptor potential cation channel subfamily V member 4 / Transient receptor potential cation channel subfamily V member 1-4 / Transient receptor potential cation channel subfamily V / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Ankyrin repeat / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Ion transport domain / Ion transport protein
Similarity search - Domain/homology
Green fluorescent protein / Transient receptor potential cation channel subfamily V member 4
Similarity search - Component
Biological speciesHomo sapiens (human) / Aequorea victoria (jellyfish)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.18 Å
AuthorsBotte M / Ulrich AKG
CitationJournal: To Be Published
Title: Cryo-EM structural studies of the agonist complexed human TRPV4 ion-channel reveals novel structural rearrangements resulting in an open-conformation
Authors: Botte M / Ulrich AKG / Adaixo R / Gnutt D / Brockmann A / Bucher D / Chami M / Bocquet M / Ebbinghaus-Kintscher U / Puetter V / Becker A / Egner U / Stahlberg H / Hennig M / Holton SJ
History
DepositionSep 3, 2020-
Header (metadata) releaseAug 18, 2021-
Map releaseAug 18, 2021-
UpdateJul 10, 2024-
Current statusJul 10, 2024Processing site: PDBe / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.148
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.148
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-7aa5
  • Surface level: 0.148
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11690.png

Downloads & links

-
Map

FileDownload / File: emd_11690.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.64 Å/pix.
x 512 pix.
= 327.168 Å		0.64 Å/pix.
x 512 pix.
= 327.168 Å		0.64 Å/pix.
x 512 pix.
= 327.168 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.639 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.148 / Movie #1: 0.148
Minimum - Maximum-0.36322987 - 0.7391092
Average (Standard dev.)0.0021438804 (±0.025488673)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 327.168 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.6390.6390.639
M x/y/z512512512
origin x/y/z0.0000.0000.000
length x/y/z327.168327.168327.168
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS512512512
D min/max/mean-0.3630.7390.002

-
Supplemental data

-
Sample components

-
Entire : Human TRPV4 in complex with 4a-PDD

EntireName: Human TRPV4 in complex with 4a-PDD
Components
  • Complex: Human TRPV4 in complex with 4a-PDD
    • Protein or peptide: Transient receptor potential cation channel subfamily V member 4,Green fluorescent protein
  • Ligand: CALCIUM ION

-
Supramolecule #1: Human TRPV4 in complex with 4a-PDD

SupramoleculeName: Human TRPV4 in complex with 4a-PDD / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

-
Macromolecule #1: Transient receptor potential cation channel subfamily V member 4,...

MacromoleculeName: Transient receptor potential cation channel subfamily V member 4,Green fluorescent protein
type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Aequorea victoria (jellyfish)
Molecular weightTheoretical: 106.24182 KDa
Recombinant expressionOrganism: Baculovirus expression vector pFastBac1-HM
SequenceString: MDYKDDDDKS SMGSRTSLYK KAGSLEVLFQ GPVFNRPILF DIVSRGSTAD LDGLLPFLLT HKKRLTDEEF REPSTGKTCL PKALLNLSN GRNDTIPVLL DIAERTGNMR EFINSPFRDI YYRGQTALHI AIERRCKHYV ELLVAQGADV HAQARGRFFQ P KDEGGYFY ...String:
MDYKDDDDKS SMGSRTSLYK KAGSLEVLFQ GPVFNRPILF DIVSRGSTAD LDGLLPFLLT HKKRLTDEEF REPSTGKTCL PKALLNLSN GRNDTIPVLL DIAERTGNMR EFINSPFRDI YYRGQTALHI AIERRCKHYV ELLVAQGADV HAQARGRFFQ P KDEGGYFY FGELPLSLAA CTNQPHIVNY LTENPHKKAD MRRQDSRGNT VLHALVAIAD NTRENTKFVT KMYDLLLLKC AR LFPDSNL EAVLNNDGLS PLMMAAKTGK IGIFQHIIRR EVTDEDTRHL SRKFKDWAYG PVYSSLYDLS SLDTCGEEAS VLE ILVYNS KIENRHEMLA VEPINELLRD KWRKFGAVSF YINVVSYLCA MVIFTLTAYY QPLEGTPPYP YRTTVDYLRL AGEV ITLFT GVLFFFTNIK DLFMKKCPGV NSLFIDGSFQ LLYFIYSVLV IVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRG LKLT GTYSIMIQKI LFKDLFRFLL VYLLFMIGYA SALVSLLNPC ANMKVCNEDQ TDCTVPTYPS CRDSETFSTF LLDLFK LTI GMGDLEMLSS TKYPVVFIIL LVTYIILTFV LLLNMLIALM GETVGQVSKE SKHIWKLQWA TTILDIERSF PVFLRKA FR SGEMVTVGKS SDGTPDRRWC FRVDEVNWSH ENLYFQGAAG SGEFKGEELF TGVVPILVEL DGDVNGHKFS VSGEGEGD A TYGKLTLKFI CTTGKLPVPW PTLVTTLTYG VQCFSRYPDH MKRHDFFKSA MPEGYVQERT ISFKDDGNYK TRAEVKFEG DTLVNRIELK GIDFKEDGNI LGHKLEYNYN SHNVYITADK QKNGIKANFK IRHNIEDGSV QLADHYQQNT PIGDGPVLLP DNHYLSTQS ALSKDPNEKR DHMVLLEFVT AAGITHGMDE LYKASGHHHH HHHHHH

UniProtKB: Transient receptor potential cation channel subfamily V member 4, Green fluorescent protein

-
Macromolecule #2: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 2 / Number of copies: 1 / Formula: CA
Molecular weightTheoretical: 40.078 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration1 mg/mL
BufferpH: 8
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.0533 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK IV / Details: blot for 3 seconds before plunging.

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.18 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 51215
Initial angle assignmentType: RANDOM ASSIGNMENT
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