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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Structure of divisome complex FtsWIQLB | |||||||||
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![]() | FtsWIQLB / Gram-negative bacteria / membrane protein / divisome / CELL CYCLE | |||||||||
Function / homology | ![]() cell septum assembly / lipid-linked peptidoglycan transporter activity / peptidoglycan glycosyltransferase / peptidoglycan glycosyltransferase activity / cell septum / serine-type D-Ala-D-Ala carboxypeptidase / FtsZ-dependent cytokinesis / serine-type D-Ala-D-Ala carboxypeptidase activity / division septum assembly / cell division site ...cell septum assembly / lipid-linked peptidoglycan transporter activity / peptidoglycan glycosyltransferase / peptidoglycan glycosyltransferase activity / cell septum / serine-type D-Ala-D-Ala carboxypeptidase / FtsZ-dependent cytokinesis / serine-type D-Ala-D-Ala carboxypeptidase activity / division septum assembly / cell division site / penicillin binding / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / cell division / proteolysis / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
![]() | Yang L / Chang S / Tang D / Dong H / Xie T / Luo B / Lu G / Zhu X / Wei X / Dong C ...Yang L / Chang S / Tang D / Dong H / Xie T / Luo B / Lu G / Zhu X / Wei X / Dong C / Zhou R / Zhang X / Tang X | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural insights into the activation of the divisome complex FtsWIQLB. Authors: Lili Yang / Yujiao Chen / Shenghai Chang / Chongrong Shen / Xin Wang / Changbin Zhang / Zhibo Zhang / Bi-Sen Ding / Zhaoming Su / Haohao Dong / Xiaodi Tang / ![]() | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 97.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 19.2 KB 19.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.9 KB | Display | ![]() |
Images | ![]() | 135.6 KB | ||
Filedesc metadata | ![]() | 6.4 KB | ||
Others | ![]() ![]() | 95.5 MB 95.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 797.8 KB | Display | ![]() |
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Full document | ![]() | 797.3 KB | Display | |
Data in XML | ![]() | 18.3 KB | Display | |
Data in CIF | ![]() | 23.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8p1uMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 0.93 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_17356_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_17356_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : divisome complex FtsWIQLB
Entire | Name: divisome complex FtsWIQLB |
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Components |
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-Supramolecule #1: divisome complex FtsWIQLB
Supramolecule | Name: divisome complex FtsWIQLB / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Cell division protein FtsL
Macromolecule | Name: Cell division protein FtsL / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 11.150034 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MSRLFVKRLP TGSFLMLLLY IGLLLSAIAV AYSTYWNRQL LNSLYSELSV RDKAQAEWGR LILEQSTWTA HSRIESLAVE QLRMRVPDP AEVRMVAP UniProtKB: Cell division protein FtsL |
-Macromolecule #2: Probable peptidoglycan glycosyltransferase FtsW
Macromolecule | Name: Probable peptidoglycan glycosyltransferase FtsW / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: peptidoglycan glycosyltransferase |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 43.793629 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MLSVLRPFPS PLLSRHGIDL DFPLLAGCLA LLGLGLVMVT SASSEVAAAQ SGNPLYFSVR HLIYLVIGLI SCGLTMMVPM ATWQRWGWK LLLVAFGLLV LVITPGIGRE VNGSMRWIGF GLFNIQPSEI AKVCVVIFMA GYLIRRQQEV RESWMGFFKP F VVLLPMAG ...String: MLSVLRPFPS PLLSRHGIDL DFPLLAGCLA LLGLGLVMVT SASSEVAAAQ SGNPLYFSVR HLIYLVIGLI SCGLTMMVPM ATWQRWGWK LLLVAFGLLV LVITPGIGRE VNGSMRWIGF GLFNIQPSEI AKVCVVIFMA GYLIRRQQEV RESWMGFFKP F VVLLPMAG LLLREPDFGA TVVMMGAAAA MLFLGGVGLF RFGLMVLLAV GAVVLLIQTQ PYRMARLTNF TDPWADQFGA GY QLSQALI AFGRGGWLGM GLGNSIQKQF YLPEAHTDFV FAVLAEELGI VGALATVALF VFVSLRALYI GIWAEQAKQF FSA YVAYGL AFLWIGQFLI NIGVNVGLLP TKGLTLPFLS YGGSSLVICC ACLGMLLRIE WERRTHLGSE EYEFNEEDFA DER UniProtKB: Probable peptidoglycan glycosyltransferase FtsW |
-Macromolecule #3: Peptidoglycan D,D-transpeptidase FtsI
Macromolecule | Name: Peptidoglycan D,D-transpeptidase FtsI / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: serine-type D-Ala-D-Ala carboxypeptidase |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 62.933082 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MKLNYFQGAL YPWRFCVIVG LLLAMVGAIV WRIVDLHVID HDFLKGQGDA RSVRHIAIPA HRGLITDRNG EPLAVSTPVT TLWANPKEL MTAKERWPQL AAALGQDTKL FADRIEQNAE REFIYLVRGL TPEQGEGVIA LKVPGVYSIE EFRRFYPAGE V VAHAVGFT ...String: MKLNYFQGAL YPWRFCVIVG LLLAMVGAIV WRIVDLHVID HDFLKGQGDA RSVRHIAIPA HRGLITDRNG EPLAVSTPVT TLWANPKEL MTAKERWPQL AAALGQDTKL FADRIEQNAE REFIYLVRGL TPEQGEGVIA LKVPGVYSIE EFRRFYPAGE V VAHAVGFT DVDDRGREGI ELAFDEWLAG VPGKRQVLKD RRGRVIKDVQ VTKNAKPGKT LALSIDLRLQ YLAHRELRNA LL ENGAKAG SLVIMDVKTG EILAMTNQPT YNPNNRRNLQ PAAMRNRAMI DVFEPGSTVK PFSMSAALAS GRWKPSDIVD VYP GTLQIG RYTIRDVSRN SRQLDLTGIL IKSSNVGISK IAFDIGAESI YSVMQQVGLG QDTGLGFPGE RVGNLPNHRK WPKA ETATL AYGYGLSVTA IQLAHAYAAL ANDGKSVPLS MTRVDRVPDG VQVISPEVAS TVQGMLQQVV EAQGGVFRAQ VPGYH AAGK SGTARKVSVG TKGYRENAYR SLFAGFAPAT DPRIAMVVVI DEPSKAGYFG GLVSAPVFSK VMAGALRLMN VPPDNL PTA TEQQQVNAAP AKGGRG UniProtKB: Peptidoglycan D,D-transpeptidase FtsI |
-Macromolecule #4: Cell division protein FtsB
Macromolecule | Name: Cell division protein FtsB / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 10.890521 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MRLRSPYWLF VVLILALAGL QYRLWVGDGS LAQVRDLQKQ IADQHGENER LLERNRILEA EVAELKKGTE TVEERARHEL GMVKDGETL YQLAK UniProtKB: Cell division protein FtsB |
-Macromolecule #5: Cell division protein FtsQ
Macromolecule | Name: Cell division protein FtsQ / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 32.290223 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MNGVLLRHQQ PGGLGRAPRK PMPRGASRLV AKEPLSVRLP KADFSFLKYL AWPLLLAVLG YGAYRGAEYI LPYADRPIAK VSVEGDLSY ISQRAVQQRI SPYLAASFFT IDLAGMRGQL EQMPWIAHAE VRRVWPDQVV IRLDEQLPIA RWGDEALLNN Q GQAFTPKE ...String: MNGVLLRHQQ PGGLGRAPRK PMPRGASRLV AKEPLSVRLP KADFSFLKYL AWPLLLAVLG YGAYRGAEYI LPYADRPIAK VSVEGDLSY ISQRAVQQRI SPYLAASFFT IDLAGMRGQL EQMPWIAHAE VRRVWPDQVV IRLDEQLPIA RWGDEALLNN Q GQAFTPKE LANYEHLPRL HGPQRAQQQV MQQYQLLSQL LRPLGFSIAR LEMSDRGGWA LTTAQGVEIQ IGRDHVVDKI RR FVSIYDK ALKDQISNIA RIDLRYPNGL AVAWREPVTP ATVATASAVQ UniProtKB: Cell division protein FtsQ |
-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 |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Calibrated defocus max: 2.0 µm / Calibrated defocus min: 1.0 µm / 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 |