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Open data
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Basic information
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| Title | Cryo-EM structure of E coli pstSCAB in the resting state | |||||||||
Map data | Cryo-EM structure of E coli pstSCAB in the resting state | |||||||||
Sample |
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Keywords | ABC transporter / Phosphate transport / pstSCAB complex / METAL TRANSPORT | |||||||||
| Function / homology | Function and homology informationABC-type phosphate transporter / ATPase-coupled phosphate ion transmembrane transporter activity / phosphate transmembrane transporter activity / phosphate ion transport / phosphate ion transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / response to radiation / DNA damage response / ATP hydrolysis activity / ATP binding ...ABC-type phosphate transporter / ATPase-coupled phosphate ion transmembrane transporter activity / phosphate transmembrane transporter activity / phosphate ion transport / phosphate ion transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / response to radiation / DNA damage response / ATP hydrolysis activity / ATP binding / membrane / plasma membrane Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||
Authors | Chen QF / Xiao H | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: Molecular mechanism of phosphate import by the bacterial PstSCAB transporter. Authors: Hu Xiao / Shanqin Li / Ruxi Qi / Yuxiang Hu / Xiaozi Jiang / Jing Luo / Jing Wu / Lei Zhang / Shuman Xu / Defen Lu / Xinwang Yang / Qingfeng Chen / Sheng Liu / ![]() Abstract: Inorganic phosphate (Pi) is essential for all living organisms. PstSCAB, a bacterial high-affinity ABC transporter, imports Pi under limiting conditions via five subunits: PstA and PstC forming the ...Inorganic phosphate (Pi) is essential for all living organisms. PstSCAB, a bacterial high-affinity ABC transporter, imports Pi under limiting conditions via five subunits: PstA and PstC forming the transmembrane domain (TMD), periplasmic PstS that switches between free and TMD-docked forms for Pi capture and delivery, and two cytosolic PstB subunits for ATP binding and hydrolysis. Its malfunction affects the virulence of pathogenic bacteria, making it pharmaceutically attractive. However, complete structural pictures of PstSCAB in different states remain lacking. Here, we determine cryo-EM structures of PstSCAB in resting, pretranslocation, and catalytic intermediate states, which reveal that conformational changes in PstS and ATP binding/unbinding in PstB collectively induce rigid-body movements of TMD, generating inward- or outward-facing conformations. In TMD, Pi specificity is determined by positively charged Arg220 (PstA) and Arg237 (PstC). This study advances understanding of bacterial Pi import and supports drug development targeting PstSCAB. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_62032.map.gz | 59.8 MB | EMDB map data format | |
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| Header (meta data) | emd-62032-v30.xml emd-62032.xml | 18.4 KB 18.4 KB | Display Display | EMDB header |
| Images | emd_62032.png | 47.4 KB | ||
| Filedesc metadata | emd-62032.cif.gz | 6.1 KB | ||
| Others | emd_62032_half_map_1.map.gz emd_62032_half_map_2.map.gz | 59.4 MB 59.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-62032 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-62032 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9k3yMC ![]() 9k3sC ![]() 9k3xC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_62032.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Cryo-EM structure of E coli pstSCAB in the resting state | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.856 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_62032_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_62032_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : pstCAB
| Entire | Name: pstCAB |
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| Components |
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-Supramolecule #1: pstCAB
| Supramolecule | Name: pstCAB / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Phosphate transport system permease protein PstA
| Macromolecule | Name: Phosphate transport system permease protein PstA / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 32.346656 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAMVEMQTTA ALAESRRKMQ ARRRLKNRIA LTLSMATMAF GLFWLIWILM STITRGIDGM SLALFTEMTP PPNTEGGGLA NALAGSGLL ILWATVFGTP LGIMAGIYLA EYGRKSWLAE VIRFINDILL SAPSIVVGLF VYTIVVAQME HFSGWAGVIA L ALLQVPIV ...String: MAMVEMQTTA ALAESRRKMQ ARRRLKNRIA LTLSMATMAF GLFWLIWILM STITRGIDGM SLALFTEMTP PPNTEGGGLA NALAGSGLL ILWATVFGTP LGIMAGIYLA EYGRKSWLAE VIRFINDILL SAPSIVVGLF VYTIVVAQME HFSGWAGVIA L ALLQVPIV IRTTENMLKL VPYSLREAAY ALGTPKWKMI SAITLKASVS GIMTGILLAI ARIAGETAPL LFTALSNQFW ST DMMQPIA NLPVTIFKFA MSPFAEWQQL AWAGVLIITL CVLLLNILAR VVFAKNKHG UniProtKB: Phosphate transport system permease protein PstA |
-Macromolecule #2: Phosphate transport system permease protein PstC
| Macromolecule | Name: Phosphate transport system permease protein PstC / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 34.138785 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAATKPAFNP PGKKGDIIFS VLVKLAALIV LLMLGGIIVS LIISSWPSIQ KFGLAFLWTK EWDAPNDIYG ALVPIYGTLV TSFIALLIA VPVSFGIALF LTELAPGWLK RPLGIAIELL AAIPSIVYGM WGLFIFAPLF AVYFQEPVGN IMSNIPIVGA L FSGPAFGI ...String: MAATKPAFNP PGKKGDIIFS VLVKLAALIV LLMLGGIIVS LIISSWPSIQ KFGLAFLWTK EWDAPNDIYG ALVPIYGTLV TSFIALLIA VPVSFGIALF LTELAPGWLK RPLGIAIELL AAIPSIVYGM WGLFIFAPLF AVYFQEPVGN IMSNIPIVGA L FSGPAFGI GILAAGVILA IMIIPYIAAV MRDVFEQTPV MMKESAYGIG CTTWEVIWRI VLPFTKNGVI GGIMLGLGRA LG ETMAVTF IIGNTYQLDS ASLYMPGNSI TSALANEFAE AESGLHVAAL MELGLILFVI TFIVLAASKF MIMRLAKNEG AR UniProtKB: Phosphate transport system permease protein PstC |
-Macromolecule #3: Phosphate import ATP-binding protein PstB
| Macromolecule | Name: Phosphate import ATP-binding protein PstB / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO / EC number: ABC-type phosphate transporter |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 29.06027 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSMVETAPSK IQVRNLNFYY GKFHALKNIN LDIAKNQVTA FIGPSGCGKS TLLRTFNKMF ELYPEQRAEG EILLDGDNIL TNSQDIALL RAKVGMVFQK PTPFPMSIYD NIAFGVRLFE KLSRADMDER VQWALTKAAL WNETKDKLHQ SGYSLSGGQQ Q RLCIARGI ...String: MSMVETAPSK IQVRNLNFYY GKFHALKNIN LDIAKNQVTA FIGPSGCGKS TLLRTFNKMF ELYPEQRAEG EILLDGDNIL TNSQDIALL RAKVGMVFQK PTPFPMSIYD NIAFGVRLFE KLSRADMDER VQWALTKAAL WNETKDKLHQ SGYSLSGGQQ Q RLCIARGI AIRPEVLLLD EPCSALDPIS TGRIEELITE LKQDYTVVIV THNMQQAARC SDHTAFMYLG ELIEFSNTDD LF TKPAKKQ TEDYITGRYG UniProtKB: Phosphate import ATP-binding protein PstB |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1 mg/mL |
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| Buffer | pH: 8 |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Protocol: AB INITIO MODEL |
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| Output model | ![]() PDB-9k3y: |
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Keywords
Authors
China, 1 items
Citation






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FIELD EMISSION GUN
