[English] 日本語
Yorodumi
- SASDEC7: Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain at pH 7.4 ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: SASBDB / ID: SASDEC7
SampleHuman TRPML2 Ion Channel Extracytosolic/Lumenal Domain at pH 7.4 without Calcium
  • Transient receptor potential channel mucolipin 2 (protein), TRPML2, Homo sapiens
Function / homology
Function and homology information


macrophage migration / positive regulation of macrophage inflammatory protein 1 alpha production / NAADP-sensitive calcium-release channel activity / iron ion transmembrane transporter activity / positive regulation of chemokine (C-C motif) ligand 5 production / neutrophil migration / positive regulation of monocyte chemotactic protein-1 production / positive regulation of chemokine (C-X-C motif) ligand 2 production / TRP channels / calcium ion transmembrane transport ...macrophage migration / positive regulation of macrophage inflammatory protein 1 alpha production / NAADP-sensitive calcium-release channel activity / iron ion transmembrane transporter activity / positive regulation of chemokine (C-C motif) ligand 5 production / neutrophil migration / positive regulation of monocyte chemotactic protein-1 production / positive regulation of chemokine (C-X-C motif) ligand 2 production / TRP channels / calcium ion transmembrane transport / calcium channel activity / recycling endosome membrane / protein transport / late endosome membrane / adaptive immune response / lysosome / innate immune response / identical protein binding / membrane / plasma membrane
Similarity search - Function
Mucolipin / : / Mucolipin, extracytosolic domain / Polycystin cation channel, PKD1/PKD2 / Polycystin cation channel
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
CitationJournal: Structure / Year: 2019
Title: Structure of the Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain.
Authors: Kerstin K Viet / Annika Wagner / Kevin Schwickert / Nils Hellwig / Martha Brennich / Nicole Bader / Tanja Schirmeister / Nina Morgner / Hermann Schindelin / Ute A Hellmich /
Abstract: TRPML2 is the least structurally characterized mammalian transient receptor potential mucolipin ion channel. The TRPML family hallmark is a large extracytosolic/lumenal domain (ELD) between ...TRPML2 is the least structurally characterized mammalian transient receptor potential mucolipin ion channel. The TRPML family hallmark is a large extracytosolic/lumenal domain (ELD) between transmembrane helices S1 and S2. We present crystal structures of the tetrameric human TRPML2 ELD at pH 6.5 (2.0 Å) and 4.5 (2.95 Å), corresponding to the pH values in recycling endosomes and lysosomes. Isothermal titration calorimetry shows Ca binding to the highly acidic central pre-pore loop which is abrogated at low pH, in line with a pH-dependent channel regulation model. Small angle X-ray scattering confirms the ELD dimensions in solution. Changes in pH or Ca concentration do not affect the protein's secondary structure, but can influence ELD oligomer integrity according to native mass spectrometry. Our data thus complete the set of high-resolution views of human TRPML channel ELDs and reveal some structural responses to the conditions the TRPML2 ELD encounters as the channel traffics through the endolysosomal system.
Contact author
  • Martha Brennich (EMBL, European Molecular Biology Laboratory (EMBL) - Grenoble Outstation, Grenoble, France)

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Models

Model #2584
Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 0.93 / P-value: 0.203262
Search similar-shape structures of this assembly by Omokage search (details)
Model #2585
Type: dummy / Radius of dummy atoms: 1.80 A / Chi-square value: 0.971 / P-value: 0.003382
Search similar-shape structures of this assembly by Omokage search (details)

-
Sample

SampleName: Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain at pH 7.4 without Calcium
Specimen concentration: 0.7 mg/ml
BufferName: 10 mM HEPES pH 7.4, 150 mM NaCl / pH: 7.4
Entity #1357Name: TRPML2 / Type: protein
Description: Transient receptor potential channel mucolipin 2
Formula weight: 23.354 / Num. of mol.: 4 / Source: Homo sapiens / References: UniProt: Q8IZK6
Sequence: GLSNQLVVAF KEDNTVAFKH LFLKGYSGTD EDDYSCSVYT QEDAYESIFF AINQYHQLKD ITLGTLGYGE NEDNRIGLKV CKQHYKKGTM FPSNETLNID NDVELDCVQL DLQDLSKKPP DWKNSSFFRL EFYRLLQVEI SFHLKGIDLQ TIHSRELPDC YVFQNTIIFD ...Sequence:
GLSNQLVVAF KEDNTVAFKH LFLKGYSGTD EDDYSCSVYT QEDAYESIFF AINQYHQLKD ITLGTLGYGE NEDNRIGLKV CKQHYKKGTM FPSNETLNID NDVELDCVQL DLQDLSKKPP DWKNSSFFRL EFYRLLQVEI SFHLKGIDLQ TIHSRELPDC YVFQNTIIFD NKAHSGKIKI YFDSDAKIEE CKDLNIFGST QK

-
Experimental information

BeamInstrument name: ESRF BM29 / City: Grenoble / : France / Type of source: X-ray synchrotron / Wavelength: 0.099 Å / Dist. spec. to detc.: 2.849 mm
DetectorName: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm
Scan
Title: Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain at pH 7.4 without Calcium
Measurement date: Oct 18, 2018 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 1200 / Unit: 1/nm /
MinMax
Q0.0354 4.9462
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 459 /
MinMax
Q0.219169 2.37769
P(R) point1 459
R0 8.9
Result
Type of curve: sec
Comments: The experimental mass was determined via correlated volume.
ExperimentalPorod
MW90 kDa83 kDa
Volume-134 nm3

P(R)GuinierGuinier error
Forward scattering, I060.3 60.22 0.13
Radius of gyration, Rg3.345 nm3.36 nm0.23

MinMax
D-8.9
Guinier point28 75

+
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