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- EMDB-10771: Engineered glycolyl-CoA carboxylase (quintuple mutant) with bound CoA -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-10771 | |||||||||
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Title | Engineered glycolyl-CoA carboxylase (quintuple mutant) with bound CoA | |||||||||
![]() | engineered glycolyl-CoA carboxylase | |||||||||
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Function / homology | ![]() propionyl-CoA carboxylase / urea carboxylase activity / propionyl-CoA carboxylase activity / methylcrotonoyl-CoA carboxylase activity / lipid catabolic process / ATP binding / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 1.96 Å | |||||||||
![]() | Schuller JM / Schuller SK / Zarzycki J / Scheffen M / Marchal DM / Erb TJ | |||||||||
Funding support | ![]()
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![]() | ![]() Title: A new-to-nature carboxylation module to improve natural and synthetic CO2 fixation Authors: Scheffen M / Marchal DG / Beneyton T / Schuller SK / Klose M / Diehl C / Lehmann J / Pfister P / Carrillo M / He H / Aslan S / Cortina NS / Claus P / Bollschweiler D / Baret JC / Schuller JM ...Authors: Scheffen M / Marchal DG / Beneyton T / Schuller SK / Klose M / Diehl C / Lehmann J / Pfister P / Carrillo M / He H / Aslan S / Cortina NS / Claus P / Bollschweiler D / Baret JC / Schuller JM / Zarzycki J / Bar-Even A / Erb TJ | |||||||||
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 | ![]() | 13.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14 KB 14 KB | Display Display | ![]() |
Images | ![]() | 221.7 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 235 KB | Display | ![]() |
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Full document | ![]() | 234.1 KB | Display | |
Data in XML | ![]() | 6.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6ybqMC ![]() 6ybpC 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 | engineered glycolyl-CoA carboxylase | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.8512 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 : Engineered glycolyl-CoA carboxylase with bound CoA
Entire | Name: Engineered glycolyl-CoA carboxylase with bound CoA |
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Components |
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-Supramolecule #1: Engineered glycolyl-CoA carboxylase with bound CoA
Supramolecule | Name: Engineered glycolyl-CoA carboxylase with bound CoA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Molecular weight | Experimental: 767 KDa |
-Macromolecule #1: Propionyl-CoA carboxylase beta chain
Macromolecule | Name: Propionyl-CoA carboxylase beta chain / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO / EC number: propionyl-CoA carboxylase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 55.963926 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MKDILEKLEE RRAQARLGGG EKRLEAQHKR GKLTARERIE LLLDHGSFEE FDMFVQHRST DFGMEKQKIP GDGVVTGWGT VNGRTVFLF SKDFTVFGGS SSEAHAAKIV KVQDMALKMR APIIGIFDAG GARIQEGVAA LGGHGEVFRR NVAASGVIPQ I SVIMGPCA ...String: MKDILEKLEE RRAQARLGGG EKRLEAQHKR GKLTARERIE LLLDHGSFEE FDMFVQHRST DFGMEKQKIP GDGVVTGWGT VNGRTVFLF SKDFTVFGGS SSEAHAAKIV KVQDMALKMR APIIGIFDAG GARIQEGVAA LGGHGEVFRR NVAASGVIPQ I SVIMGPCA GGDVYSPAMT DFIFMVRDTS YMFVTGPDVV KTVTNEVVTA EELGGAKVHT SKSSIADGSF ENDVEAILQI RR LLDFLPA NNIEGVPEIE SFDDVNRLDK SLDTLIPDNP NKPYDMGELI RRVVDEGDFF EIQAAYARNI ITGFGRVEGR TVG FVANQP LVLAGVLDSD ASRKAARFVR FCNAFSIPIV TFVDVPGFLP GTAQEYGGLI KHGAKLLFAY SQATVPLVTI ITRK AFGGA YIVMASKHVG ADLNYAWPTA QIAVMGAKGA VEIIFRAEIG DADKVAERTK EYEDRFLSPF VAAERGYIDE VIMPH STRK RIARALGMLR TKEMEQPRKK HDNIPL |
-Macromolecule #2: Propionyl-CoA carboxylase alpha subunit
Macromolecule | Name: Propionyl-CoA carboxylase alpha subunit / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO / EC number: propionyl-CoA carboxylase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 71.986961 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MFDKILIANR GEIACRIIKT AQKMGIKTVA VYSDADRDAV HVAMADEAVH IGPAPAAQSY LLIEKIIDAC KQTGAQAVHP GYGFLSERE SFPKALAEAG IVFIGPNPGA IAAMGDKIES KKAAAAAEVS TVPGFLGVIE SPEHAVTIAD EIGYPVMIKA S AGGGGKGM ...String: MFDKILIANR GEIACRIIKT AQKMGIKTVA VYSDADRDAV HVAMADEAVH IGPAPAAQSY LLIEKIIDAC KQTGAQAVHP GYGFLSERE SFPKALAEAG IVFIGPNPGA IAAMGDKIES KKAAAAAEVS TVPGFLGVIE SPEHAVTIAD EIGYPVMIKA S AGGGGKGM RIAESADEVA EGFARAKSEA SSSFGDDRVF VEKFITDPRH IEIQVIGDKH GNVIYLGERE CSIQRRNQKV IE EAPSPLL DEETRRKMGE QAVALAKAVN YDSAGTVEFV AGQDKSFYFL EMNTRLQVEH PVTEMITGLD LVELMIRVAA GEK LPLSQD QVKLDGWAVE SRVYAEDPTR NFLPSIGRLT TYQPPEEGPL GGAIVRNDTG VEEGGEIAIH YDPMIAKLVT WAPT RLEAI EAQATALDAF AIEGIRHNIP FLATLMAHPR WRDGRLSTGF IKEEFPEGFI APEPEGPVAH RLAAVAAAID HKLNI RKRG ISGQMRDPSL LTFQRERVVV LSGQRFNVTV DPDGDDLLVT FDDGTTAPVR SAWRPGAPVW SGTVGDQSVA IQVRPL LNG VFLQHAGAAA EARVFTRREA ELADLMPVKE NAGSGKQLLC PMPGLVKQIM VSEGQEVKNG EPLAIVEAMK MENVLRA ER DGTISKIAAK EGDSLAVDAV ILEFA |
-Macromolecule #3: COENZYME A
Macromolecule | Name: COENZYME A / type: ligand / ID: 3 / Number of copies: 6 / Formula: COA |
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Molecular weight | Theoretical: 767.534 Da |
Chemical component information | ![]() ChemComp-COA: |
-Macromolecule #4: 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL
Macromolecule | Name: 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL type: ligand / ID: 4 / Number of copies: 6 / Formula: BTI |
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Molecular weight | Theoretical: 228.311 Da |
Chemical component information | ![]() ChemComp-BTI: |
-Macromolecule #5: water
Macromolecule | Name: water / type: ligand / ID: 5 / Number of copies: 871 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ![]() ChemComp-HOH: |
-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: 7.8 |
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Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 55.0 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 |
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Image processing
Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 1.96 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 2181317 |
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Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: PROJECTION MATCHING |