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Open data
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Basic information
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| Title | Human FAM118B(34-334) 2 protomers | |||||||||
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Sample |
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Keywords | NADase / HYDROLASE | |||||||||
| Function / homology | Protein FAM118 / SIR2-like domain / Cajal body / identical protein binding / Protein FAM118B Function and homology information | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.8 Å | |||||||||
Authors | Missoury S / Coste F / Baretic D / Patel K / Delarue M / Ahel I / Suskiewicz MJ | |||||||||
| Funding support | 1 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2025Title: Filament formation and NAD processing by noncanonical human FAM118 sirtuins. Authors: Domagoj Baretić / Sophia Missoury / Karishma Patel / Maximilien Martinez / Franck Coste / Kang Zhu / Rebecca Smith / Anna Georgina Kopasz / Yang Lu / Nicolas Bigot / Catherine Chapuis / ...Authors: Domagoj Baretić / Sophia Missoury / Karishma Patel / Maximilien Martinez / Franck Coste / Kang Zhu / Rebecca Smith / Anna Georgina Kopasz / Yang Lu / Nicolas Bigot / Catherine Chapuis / Romane Riou / Nina Đukić / Stéphane Goffinont / Valentin Pressoir / Sara Patačko / Gyula Timinszky / Marc Delarue / Bertrand Castaing / Dragana Ahel / Andreja Mikoč / Sébastien Huet / Ivan Ahel / Marcin J Suskiewicz / ![]() Abstract: Sirtuins are an ancient family of enzymes with diverse nicotinamide adenine dinucleotide (NAD)-dependent activities. Here we identify family with sequence similarity 118 member B (FAM118B) and ...Sirtuins are an ancient family of enzymes with diverse nicotinamide adenine dinucleotide (NAD)-dependent activities. Here we identify family with sequence similarity 118 member B (FAM118B) and FAM118A-two understudied vertebrate proteins-as vertebrate-specific sirtuins with similarities to bacterial antiphage sirtuins. We show that human FAM118B forms head-to-tail filaments both in vitro and in living human cells, a feature that appears to be conserved in both FAM118B and its paralog FAM118A across vertebrates. While human FAM118B and FAM118A have individually very weak NAD-processing activity in vitro, their interaction leads to markedly increased activity, suggesting a tightly regulated system. The overexpression of wild-type human FAM118B and FAM118A leads to strongly decreased NAD levels in human cells, an effect that is abolished in catalytically dead or filament-deficient mutants. Our study highlights filament formation and NAD processing as conserved mechanisms among immunity-associated sirtuins across evolution. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_53555.map.gz | 483.4 MB | EMDB map data format | |
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| Header (meta data) | emd-53555-v30.xml emd-53555.xml | 18.1 KB 18.1 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_53555_fsc.xml | 23.6 KB | Display | FSC data file |
| Images | emd_53555.png | 13.4 KB | ||
| Filedesc metadata | emd-53555.cif.gz | 6.2 KB | ||
| Others | emd_53555_half_map_1.map.gz emd_53555_half_map_2.map.gz | 474.5 MB 474.5 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-53555 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-53555 | HTTPS FTP |
-Validation report
| Summary document | emd_53555_validation.pdf.gz | 831.6 KB | Display | EMDB validaton report |
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| Full document | emd_53555_full_validation.pdf.gz | 831.2 KB | Display | |
| Data in XML | emd_53555_validation.xml.gz | 25.3 KB | Display | |
| Data in CIF | emd_53555_validation.cif.gz | 34 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-53555 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-53555 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9r3eMC ![]() 9r0pC ![]() 9r0sC 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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Map
| File | Download / File: emd_53555.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.839 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_53555_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_53555_half_map_2.map | ||||||||||||
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Sample components
-Entire : Human FAM118B(24-334) focused trimer filament
| Entire | Name: Human FAM118B(24-334) focused trimer filament |
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| Components |
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-Supramolecule #1: Human FAM118B(24-334) focused trimer filament
| Supramolecule | Name: Human FAM118B(24-334) focused trimer filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Protein FAM118B
| Macromolecule | Name: Protein FAM118B / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 34.08716 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: PRKLLPSLKT KKPRELVLVI GTGISAAVAP QVPALKSWKG LIQALLDAAI DFDLLEDEES KKFQKCLHED KNLVHVAHDL IQKLSPRTS NVRSTFFKDC LYEVFDDLES KMEDSGKQLL QSVLHLMENG ALVLTTNFDN LLELYAADQG KQLESLDLTD E KKVLEWAQ ...String: PRKLLPSLKT KKPRELVLVI GTGISAAVAP QVPALKSWKG LIQALLDAAI DFDLLEDEES KKFQKCLHED KNLVHVAHDL IQKLSPRTS NVRSTFFKDC LYEVFDDLES KMEDSGKQLL QSVLHLMENG ALVLTTNFDN LLELYAADQG KQLESLDLTD E KKVLEWAQ EKRKLSVLHI HGVYTNPSGI VLHPAGYQNV LRNTEVMREI QKLYENKSFL FLGCGWTVDD TTFQALFLEA VK HKSDLEH FMLVRRGDVD EFKKLRENML DKGIKVISYG DDYADLPEYF KRLTCEISTR G UniProtKB: Protein FAM118B |
-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 | 0.1 mg/mL |
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| Buffer | pH: 8.8 / Details: 25 mM Tris, pH 8.8, 250 mM NaCl, 0.5 mM TCEP |
| Grid | Model: EMS Lacey Carbon / Material: COPPER / Mesh: 200 / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Atmosphere: OTHER |
| Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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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: 42.0 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: 2.8000000000000003 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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| Output model | ![]() PDB-9r3e: |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
Citation






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FIELD EMISSION GUN

