[English] 日本語
![](img/lk-miru.gif)
- EMDB-22724: CryoEM structure of a trehalose monomycolate transporter in lipid... -
+
Open data
-
Basic information
Entry | Database: EMDB / ID: EMD-22724 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | CryoEM structure of a trehalose monomycolate transporter in lipid nanodiscs | |||||||||
![]() | ||||||||||
![]() |
| |||||||||
![]() | trehalose monomycolate transporter / TRANSLOCASE | |||||||||
Function / homology | ![]() phosphatidylethanolamine transfer activity / phosphatidylglycerol binding / trehalose transmembrane transporter activity / trehalose transport / mycolate cell wall layer assembly / diacylglycerol binding / cell wall biogenesis / cell pole / cell tip / mycolic acid biosynthetic process ...phosphatidylethanolamine transfer activity / phosphatidylglycerol binding / trehalose transmembrane transporter activity / trehalose transport / mycolate cell wall layer assembly / diacylglycerol binding / cell wall biogenesis / cell pole / cell tip / mycolic acid biosynthetic process / cell septum / phospholipid transport / phosphatidylethanolamine binding / cardiolipin binding / phosphatidylinositol binding / regulation of membrane potential / cell wall organization / response to xenobiotic stimulus / response to antibiotic / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.65 Å | |||||||||
![]() | Su C-C | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport. Authors: Chih-Chia Su / Philip A Klenotic / Meng Cui / Meinan Lyu / Christopher E Morgan / Edward W Yu / ![]() Abstract: The mycobacterial membrane protein large 3 (MmpL3) transporter is essential and required for shuttling the lipid trehalose monomycolate (TMM), a precursor of mycolic acid (MA)-containing trehalose ...The mycobacterial membrane protein large 3 (MmpL3) transporter is essential and required for shuttling the lipid trehalose monomycolate (TMM), a precursor of mycolic acid (MA)-containing trehalose dimycolate (TDM) and mycolyl arabinogalactan peptidoglycan (mAGP), in Mycobacterium species, including Mycobacterium tuberculosis and Mycobacterium smegmatis. However, the mechanism that MmpL3 uses to facilitate the transport of fatty acids and lipidic elements to the mycobacterial cell wall remains elusive. Here, we report 7 structures of the M. smegmatis MmpL3 transporter in its unbound state and in complex with trehalose 6-decanoate (T6D) or TMM using single-particle cryo-electron microscopy (cryo-EM) and X-ray crystallography. Combined with calculated results from molecular dynamics (MD) and target MD simulations, we reveal a lipid transport mechanism that involves a coupled movement of the periplasmic domain and transmembrane helices of the MmpL3 transporter that facilitates the shuttling of lipids to the mycobacterial cell wall. | |||||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
-
Downloads & links
-EMDB archive
Map data | ![]() | 3.9 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 10.4 KB 10.4 KB | Display Display | ![]() |
Images | ![]() | 115.9 KB | ||
Filedesc metadata | ![]() | 5.6 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7k8aMC ![]() 7k7mC ![]() 7k8bC ![]() 7k8cC ![]() 7k8dC ![]() 7n6bC M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data |
-
Links
EMDB pages | ![]() ![]() |
---|
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-
Sample components
-Entire : RDN family transporter
Entire | Name: RDN family transporter |
---|---|
Components |
|
-Supramolecule #1: RDN family transporter
Supramolecule | Name: RDN family transporter / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
---|---|
Source (natural) | Organism: ![]() |
-Macromolecule #1: Drug exporters of the RND superfamily-like protein
Macromolecule | Name: Drug exporters of the RND superfamily-like protein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 110.338109 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MFAWWGRTVY QFRYIVIGVM VALCLGGGVY GISLGNHVTQ SGFYDEGSQS VAASLIGDEV YGRDRTSHVV AILTPPDDKK VTDKAWQKK VTEELDQVVK DHEDQIVGWV GWLKAPDTTD PTVSAMKTQD LRHTFISIPL QGDDDDEILK NYQVVEPELQ Q VNGGDIRL ...String: MFAWWGRTVY QFRYIVIGVM VALCLGGGVY GISLGNHVTQ SGFYDEGSQS VAASLIGDEV YGRDRTSHVV AILTPPDDKK VTDKAWQKK VTEELDQVVK DHEDQIVGWV GWLKAPDTTD PTVSAMKTQD LRHTFISIPL QGDDDDEILK NYQVVEPELQ Q VNGGDIRL AGLNPLASEL TGTIGEDQKR AEVAAIPLVA VVLFFVFGTV IAAALPAIIG GLAIAGALGI MRLVAEFTPV HF FAQPVVT LIGLGIAIDY GLFIVSRFRE EIAEGYDTEA AVRRTVMTSG RTVVFSAVII VASSVPLLLF PQGFLKSITY AII ASVMLA AILSITVLAA ALAILGPRVD ALGVTTLLKI PFLANWQFSR RIIDWFAEKT QKTKTREEVE RGFWGRLVNV VMKR PIAFA APILVVMVLL IIPLGQLSLG GISEKYLPPD NAVRQSQEQF DKLFPGFRTE PLTLVMKRED GEPITDAQIA DMRAK ALTV SGFTDPDNDP EKMWKERPAN DSGSKDPSVR VIQNGLENRN DAAKKIDELR ALQPPHGIEV FVGGTPALEQ DSIHSL FDK LPLMALILIV TTTVLMFLAF GSVVLPIKAA LMSALTLGST MGILTWMFVD GHGSGLMNYT PQPLMAPMIG LIIAVIW GL STDYEVFLVS RMVEARERGM STAEAIRIGT ATTGRLITGA ALILAVVAGA FVFSDLVMMK YLAFGLLIAL LLDATIIR M FLVPAVMKLL GDDCWWAPRW MKRVQEKLGL GETELPDERK RPTVRESETD QRALVGVGAP PPPPRPHDPT HPAPEPVRP MPPMRSNAPS AAGTARISTP PQPPQPPQAP AQQAGDEPAT TRFAMARNAV RNAVNSAVHG GAGSAAAPTE RAPRPGGPAQ PPAPPQREE REIESWLGAL RGPAPAKNVP QPPAQPQRPS TDTTRAMPPQ GRPPAGPADR GNENAPTTAF SAQRPPNGGA P ADATTAIP TPPQREQEPS TEKLNTREDA PEDPETKRRG GGMSAQDLLR REGRLHHHHH H UniProtKB: Trehalose monomycolate exporter MmpL3 |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Concentration | 0.2 mg/mL | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Buffer | pH: 7.5 Component:
| |||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
-
Image processing
Startup model | Type of model: NONE |
---|---|
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.65 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 75398 |
Initial angle assignment | Type: NOT APPLICABLE |
Final angle assignment | Type: ANGULAR RECONSTITUTION |