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- SASDEH7: Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain at pH 4.5,... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDEH7 |
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![]() | Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain at pH 4.5, 0.5 mM Calcium
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Function / homology | ![]() positive regulation of macrophage inflammatory protein 1 alpha production / NAADP-sensitive calcium-release channel activity / macrophage migration / 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 channel activity ...positive regulation of macrophage inflammatory protein 1 alpha production / NAADP-sensitive calcium-release channel activity / macrophage migration / 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 channel activity / calcium ion transmembrane transport / recycling endosome membrane / late endosome membrane / protein transport / adaptive immune response / lysosome / innate immune response / identical protein binding / membrane / plasma membrane Similarity search - Function |
Biological species | ![]() |
![]() | ![]() 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. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Models
Model #2595 | ![]() Type: atomic / Radius of dummy atoms: 1.90 A / Symmetry: P2 / Chi-square value: 1.30 / P-value: 0.000007 ![]() |
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Model #2596 | ![]() Type: dummy / Radius of dummy atoms: 2.00 A / Symmetry: P42 / Chi-square value: 4.637 ![]() |
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Sample
![]() | Name: Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain at pH 4.5, 0.5 mM Calcium Specimen concentration: 0.5 mg/ml |
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Buffer | Name: 10 mM Hepes, pH 4.5, 150 mM NaCl, 0.5 mM CaCl2 / pH: 4.5 |
Entity #1358 | Name: TRPML2 / Type: protein Description: Transient receptor potential channel mucolipin 2 Formula weight: 23.354 / Num. of mol.: 8 / 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
Beam | Instrument name: ESRF BM29 / City: Grenoble / 国: France ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm | ||||||||||||||||||||||||||||||
Scan | Measurement date: Oct 20, 2018 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 1200 / Unit: 1/nm /
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Distance distribution function P(R) |
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Result | Comments: The experimental mass was determined via correlated volume.
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