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Open data
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Basic information
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Title | Structure of E.coli Septu (PtuAB) complex | |||||||||
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![]() | PtuA / PtuB Septu / ![]() | |||||||||
Function / homology | Retron Ec78 putative HNH endonuclease-like / TIGR02646 family protein![]() | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Shen ZF / Fu TM | |||||||||
Funding support | 1 items
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![]() | ![]() Title: PtuA and PtuB assemble into an inflammasome-like oligomer for anti-phage defense. Authors: Yuanyuan Li / Zhangfei Shen / Mengyuan Zhang / Xiao-Yuan Yang / Sean P Cleary / Jiale Xie / Ila A Marathe / Marius Kostelic / Jacelyn Greenwald / Anthony D Rish / Vicki H Wysocki / Chong ...Authors: Yuanyuan Li / Zhangfei Shen / Mengyuan Zhang / Xiao-Yuan Yang / Sean P Cleary / Jiale Xie / Ila A Marathe / Marius Kostelic / Jacelyn Greenwald / Anthony D Rish / Vicki H Wysocki / Chong Chen / Qiang Chen / Tian-Min Fu / Yamei Yu / ![]() ![]() Abstract: Escherichia coli Septu system, an anti-phage defense system, comprises two components: PtuA and PtuB. PtuA contains an ATPase domain, while PtuB is predicted to function as a nuclease. Here we show ...Escherichia coli Septu system, an anti-phage defense system, comprises two components: PtuA and PtuB. PtuA contains an ATPase domain, while PtuB is predicted to function as a nuclease. Here we show that PtuA and PtuB form a stable complex with a 6:2 stoichiometry. Cryo-electron microscopy structure of PtuAB reveals a distinctive horseshoe-like configuration. PtuA adopts a hexameric arrangement, organized as an asymmetric trimer of dimers, contrasting the ring-like structure by other ATPases. Notably, the three pairs of PtuA dimers assume distinct conformations and fulfill unique roles in recruiting PtuB. Our functional assays have further illuminated the importance of the oligomeric assembly of PtuAB in anti-phage defense. Moreover, we have uncovered that ATP molecules can directly bind to PtuA and inhibit the activities of PtuAB. Together, the assembly and function of the Septu system shed light on understanding other ATPase-containing systems in bacterial immunity. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 2.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.3 KB 13.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.4 KB | Display | ![]() |
Images | ![]() | 69.3 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() | 21.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8eeaMC ![]() 8ee4C ![]() 8ee7C ![]() 8suxC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Voxel size | X=Y=Z: 1.12 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: #1
File | emd_28049_additional_1.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : 6 PtuA and 2 PtuB form as a complex
Entire | Name: 6 PtuA and 2 PtuB form as a complex |
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Components |
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-Supramolecule #1: 6 PtuA and 2 PtuB form as a complex
Supramolecule | Name: 6 PtuA and 2 PtuB form as a complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() ![]() ![]() |
-Macromolecule #1: PtuA
Macromolecule | Name: PtuA / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 53.189656 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MRIDKLSLLN FRCFKQLDIT FDEHITILVA PNGAGKTTVL DAVRLALFPF IRGFDASLYV KDKSLAIRTE DLRLIYRQEA LNMEMSSPA KITATGEWAS GKTATWMLDK RGEQPPHEDK MAAQLTRWGE QLQKRVREEH SLQQVELPLM LYLGTARLWY Q ERYEKQPT ...String: MRIDKLSLLN FRCFKQLDIT FDEHITILVA PNGAGKTTVL DAVRLALFPF IRGFDASLYV KDKSLAIRTE DLRLIYRQEA LNMEMSSPA KITATGEWAS GKTATWMLDK RGEQPPHEDK MAAQLTRWGE QLQKRVREEH SLQQVELPLM LYLGTARLWY Q ERYEKQPT EQRLDNSAFS RLSGYDDCLS ATSNYKQFEQ WYSWLWLSYR EHQITQLESP SAKLKEGVRV QRMKEAIQAI QQ AINCLTQ QVTGWHDLEY SASHNQQLVM SHPQYGKIPL SQLSDGLRNA VAMVADIAFR CVKLNPHLQN DAALKTQGIV LID EVDMFL HPAWQQQIIQ SLRSAFPQIQ FIVTTHSPQV LSTVKRESIR LLEQDENGNG KALMPLGATY GEPSNDVLQS VMGV DPQPA VKEKADLQKL TGWVDQGKYD EPKTQQLMVA LEVALGEKHP QLQRLQRSIA RQRLLKGKAQ |
-Macromolecule #2: PtuB
Macromolecule | Name: PtuB / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 28.136291 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MRHVIKTQLG TVALLTAHEN PPQDADQSTR RWRNFRRDKA AVMVQLINEQ YHLCCYSEIR SDLRGLGYHI EHVENKSQHP ERTFDYQNL AASALDSGEN GGLSSLKGKN AFGGHAQGKQ DVVDMAKFIH CHIRDCSRYF AYLSDGRIVP ADELNAQETE N AQYTIDLL ...String: MRHVIKTQLG TVALLTAHEN PPQDADQSTR RWRNFRRDKA AVMVQLINEQ YHLCCYSEIR SDLRGLGYHI EHVENKSQHP ERTFDYQNL AASALDSGEN GGLSSLKGKN AFGGHAQGKQ DVVDMAKFIH CHIRDCSRYF AYLSDGRIVP ADELNAQETE N AQYTIDLL NLNSGFLQTE RRNHWEELEQ LFDEHIEKDW DLQQLLQLDL VSTPDHKLHE FFSITRQFFQ QEAEQVLQSH AP ALI UniProtKB: TIGR02646 family protein |
-Macromolecule #3: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 4 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ![]() ChemComp-ATP: |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |