+
Open data
-
Basic information
Entry | ![]() | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of MxaF/MxaJ/PQQ complex | |||||||||
![]() | ||||||||||
![]() |
| |||||||||
![]() | MxaF/MxaJ/PQQ / PROTEIN BINDING | |||||||||
Function / homology | ![]() methanol catabolic process / Oxidoreductases; Acting on the CH-OH group of donors; With a cytochrome as acceptor / oxidoreductase activity, acting on CH-OH group of donors / outer membrane-bounded periplasmic space / periplasmic space / calcium ion binding / membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.81 Å | |||||||||
![]() | Sun JQ / Gao F | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: Cryo-EM structure of MxaF/MxaJ complex Authors: Sun JQ / Gao F | |||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 89 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 15.7 KB 15.7 KB | Display Display | ![]() |
Images | ![]() | 49.3 KB | ||
Filedesc metadata | ![]() | 5.8 KB | ||
Others | ![]() ![]() | 165.4 MB 165.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 15 KB | Display | |
Data in CIF | ![]() | 17.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9isoMC ![]() 9ismC M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
EMDB pages | ![]() ![]() |
---|
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.89 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Half map: #1
File | emd_60840_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #2
File | emd_60840_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
-Entire : MxaF/MxaJ/PQQ complex
Entire | Name: MxaF/MxaJ/PQQ complex |
---|---|
Components |
|
-Supramolecule #1: MxaF/MxaJ/PQQ complex
Supramolecule | Name: MxaF/MxaJ/PQQ complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
---|---|
Source (natural) | Organism: ![]() |
-Macromolecule #1: Methanol dehydrogenase, alpha subunit
Macromolecule | Name: Methanol dehydrogenase, alpha subunit / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO EC number: Oxidoreductases; Acting on the CH-OH group of donors; With a cytochrome as acceptor |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 69.335836 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MSRFVTSVSA LAMLALAPAA LSSGAYANDK LVELSKSDDN WVMPGKNYDS NNFSDLKQIN KGNVKQLRPA WTFSTGLLNG HEGAPLVVD GKMYIHTSFP NNTFALGLDD PGTILWQDKP KQNPAARAVA CCDLVNRGLA YWPGDGKTPA LILKTQLDGN V AALNAETG ...String: MSRFVTSVSA LAMLALAPAA LSSGAYANDK LVELSKSDDN WVMPGKNYDS NNFSDLKQIN KGNVKQLRPA WTFSTGLLNG HEGAPLVVD GKMYIHTSFP NNTFALGLDD PGTILWQDKP KQNPAARAVA CCDLVNRGLA YWPGDGKTPA LILKTQLDGN V AALNAETG ETVWKVENSD IKVGSTLTIA PYVVKDKVII GSSGAELGVR GYLTAYDVKT GEQVWRAYAT GPDKDLLLAS DF NIKNPHY GQKGLGTGTW EGDAWKIGGG TNWGWYAYDP GTNLIYFGTG NPAPWNETMR PGDNKWTMTI FGRDADTGEA KFG YQKTPH DEWDYAGVNV MMLSEQKDKD GKARKLLTHP DRNGIVYTLD RTDGALVSAN KLDDTVNVFK SVDLKTGQPV RDPE YGTRM DHLAKDICPS AMGYHNQGHD SYDPKRELFF MGINHICMDW EPFMLPYRAG QFFVGATLNM YPGPKGDRQN YEGLG QIKA YNAITGDYKW EKMERFAVWG GTMATAGDLV FYGTLDGYLK ARDSDTGDLL WKFKIPSGAI GYPMTYTHKG TQYVAI YYG VGGWPGVGLV FDLADPTAGL GAVGAFKKLA NYTQMGGGVV VFSLDGKGPY DDPNVGEWKS AAKHHHHHH UniProtKB: Methanol dehydrogenase, alpha subunit |
-Macromolecule #2: Methanol oxidation protein MxaJ
Macromolecule | Name: Methanol oxidation protein MxaJ / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 32.468154 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MSLVNGRRRT AASVVALTAA LTALAALCAP AQAQDTKATS KAAEAAKPDA GTLRVCAAEQ PPLSMKDGSG LENRIATTVA EAMGRKAQF VWLGKPAIYL VRDGLEKKTC DVVIGLDADD PRVLTSKPYY RSGYVFLTRA DKDLDIKSWS DPRLKEVSHM V VGFGTPGE ...String: MSLVNGRRRT AASVVALTAA LTALAALCAP AQAQDTKATS KAAEAAKPDA GTLRVCAAEQ PPLSMKDGSG LENRIATTVA EAMGRKAQF VWLGKPAIYL VRDGLEKKTC DVVIGLDADD PRVLTSKPYY RSGYVFLTRA DKDLDIKSWS DPRLKEVSHM V VGFGTPGE AMLKDIGRYE EDMAYLYSLV NFRAPRNQYT QIDPARMVSE VATGKAEVGV AFGPDVARYV RDSSTKLRMT PV PDDTQAS DGRKMPQSFD QAMGVRKDDT ALKAEIDAAL EKAKPKIEAI LKEEGVPVLP VSN UniProtKB: Methanol oxidation protein MxaJ |
-Macromolecule #3: PYRROLOQUINOLINE QUINONE
Macromolecule | Name: PYRROLOQUINOLINE QUINONE / type: ligand / ID: 3 / Number of copies: 2 / Formula: PQQ |
---|---|
Molecular weight | Theoretical: 330.206 Da |
Chemical component information | ![]() ChemComp-PQQ: |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 8 |
---|---|
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |