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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-21041 | |||||||||
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Title | Structure of TrkH-TrkA in complex with ATP | |||||||||
![]() | Structure of TrkH-TrkA in complex with ATP | |||||||||
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![]() | Ion channel / TRANSPORT PROTEIN | |||||||||
Function / homology | ![]() potassium:chloride symporter activity / potassium ion transmembrane transporter activity / potassium ion binding / potassium channel activity / potassium ion transmembrane transport / nucleotide binding / protein homodimerization activity / metal ion binding / identical protein binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.97 Å | |||||||||
![]() | Zhou M / Zhang H | |||||||||
Funding support | ![]()
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![]() | ![]() Title: TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential. Authors: Hanzhi Zhang / Yaping Pan / Liya Hu / M Ashley Hudson / Katrina S Hofstetter / Zhichun Xu / Mingqiang Rong / Zhao Wang / B V Venkataram Prasad / Steve W Lockless / Wah Chiu / Ming Zhou / ![]() Abstract: TrkH is a bacterial ion channel implicated in K uptake and pH regulation. TrkH assembles with its regulatory protein, TrkA, which closes the channel when bound to ADP and opens it when bound to ATP. ...TrkH is a bacterial ion channel implicated in K uptake and pH regulation. TrkH assembles with its regulatory protein, TrkA, which closes the channel when bound to ADP and opens it when bound to ATP. However, it is unknown how nucleotides control the gating of TrkH through TrkA. Here we report the structures of the TrkH-TrkA complex in the presence of ADP or ATP. TrkA forms a tetrameric ring when bound to ADP and constrains TrkH to a closed conformation. The TrkA ring splits into two TrkA dimers in the presence of ATP and releases the constraints on TrkH, resulting in an open channel conformation. Functional studies show that both the tetramer-to-dimer conversion of TrkA and the loss of constraints on TrkH are required for channel gating. In addition, deletion of TrkA in Escherichia coli depolarizes the cell, suggesting that the TrkH-TrkA complex couples changes in intracellular nucleotides to membrane potential. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 38 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.6 KB 13.6 KB | Display Display | ![]() |
Images | ![]() | 118.9 KB | ||
Filedesc metadata | ![]() | 6.2 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6v4jMC ![]() 6v4kC ![]() 6v4lC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Structure of TrkH-TrkA in complex with ATP | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.242 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : TrkH-TrkA
Entire | Name: TrkH-TrkA |
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Components |
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-Supramolecule #1: TrkH-TrkA
Supramolecule | Name: TrkH-TrkA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 400 KDa |
-Macromolecule #1: Trk system potassium uptake protein TrkH
Macromolecule | Name: Trk system potassium uptake protein TrkH / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() Strain: RIMD 2210633 |
Molecular weight | Theoretical: 53.104375 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MQFRSIIRIV GLLLALFSVT MLAPALVALL YRDGAGVPFV TTFFVLLFCG AMCWFPNRRH KHELKSRDGF LIVVLFWTVL GSAGSLPFL IADNPNISVT DAFFESFSAL TTTGATVIVG LDELPKAILF YRQFLQWFGG MGIIVLAVAI LPVLGIGGMQ L YRAEIPGP ...String: MQFRSIIRIV GLLLALFSVT MLAPALVALL YRDGAGVPFV TTFFVLLFCG AMCWFPNRRH KHELKSRDGF LIVVLFWTVL GSAGSLPFL IADNPNISVT DAFFESFSAL TTTGATVIVG LDELPKAILF YRQFLQWFGG MGIIVLAVAI LPVLGIGGMQ L YRAEIPGP VKDTKMTPRI AETAKALWYI YLSLTIACAV AFWLAGMTPF DAISHSFSTI AIGGFSTHDA SMGYFDSYAI NL ITVVFLL ISACNFTLHF AAFASGGVHP KYYWKDPEFR AFIFIQVLLF LVCFLLLLKH HSYTSPYDAF DQALFQTVSI STT AGFTTT GFADWPLFLP VLLLFSSFIG GCAGSTGGGM KVIRILLLTL QGARELKRLV HPRAVYTIKV GGSALPQRVV DAVW GFFSA YALVFVVCML GLIATGMDEL SAFSAVAATL NNLGPGLGEV ALHFGDVNDK AKWVLIVSML FGRLEIFTLL ILLTP TFWR S UniProtKB: Trk system potassium uptake protein TrkH |
-Macromolecule #2: Potassium uptake protein TrkA
Macromolecule | Name: Potassium uptake protein TrkA / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() Strain: RIMD 2210633 |
Molecular weight | Theoretical: 50.193086 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MKIIILGAGQ VGGTLAENLV GENNDITIVD NNADRLRELQ DKYDLRVVNG HASHPDVLHE AGAQDADMLV AVTNTDETNM AACQVAFTL FNTPNRVARI RSPEYLAEKE ALFKSGAIPV DHLIAPEELV TSYIERLIQY PGALQVVSFA EQKVSLVAVK A YYGGPLVG ...String: MKIIILGAGQ VGGTLAENLV GENNDITIVD NNADRLRELQ DKYDLRVVNG HASHPDVLHE AGAQDADMLV AVTNTDETNM AACQVAFTL FNTPNRVARI RSPEYLAEKE ALFKSGAIPV DHLIAPEELV TSYIERLIQY PGALQVVSFA EQKVSLVAVK A YYGGPLVG NALSALREHM PHIDTRVAAI FRQGRPIRPQ GTTIIEADDE VFFVAASNHI RSVMSELQRL EKPYRRIMIV GG GNIGASL AKRLEQTYSV KLIERDYQRA EKLSEQLENT IVFCGDAADQ ELLTEENIDQ VDVFIALTNE DETNIMSAML AKR MGAKKV MVLIQRGAYV DLVQGGVIDV AISPQQATIS ALLTHVRRAD IVNVSSLRRG AAEAIEAVAH GDETTSKVVG RAIG DIKLP PGTTIGAVVR GEEVLIAHDR TVIEQDDHVV MFLVDKKYVP DVEALFQPSP FFL UniProtKB: Trk system potassium uptake protein TrkA |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Grid | Details: unspecified |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | JEOL 3200FSC |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 80.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |