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Yorodumi- EMDB-18436: Cryo-EM Structure of Human Serine Hydroxymethyltransferase, isofo... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-18436 | |||||||||
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Title | Cryo-EM Structure of Human Serine Hydroxymethyltransferase, isoform 2 (SHMT2) | |||||||||
Map data | ||||||||||
Sample |
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Keywords | one-carbon metabolism / folate cycle / tetrahydtofolate / mitochondria / TRANSFERASE | |||||||||
Function / homology | Function and homology information BRISC complex / L-allo-threonine aldolase activity / regulation of mitochondrial translation / L-serine metabolic process / glycine metabolic process / L-serine biosynthetic process / glycine hydroxymethyltransferase / glycine hydroxymethyltransferase activity / glycine biosynthetic process from serine / Metabolism of folate and pterines ...BRISC complex / L-allo-threonine aldolase activity / regulation of mitochondrial translation / L-serine metabolic process / glycine metabolic process / L-serine biosynthetic process / glycine hydroxymethyltransferase / glycine hydroxymethyltransferase activity / glycine biosynthetic process from serine / Metabolism of folate and pterines / regulation of oxidative phosphorylation / tetrahydrofolate metabolic process / response to type I interferon / protein K63-linked deubiquitination / tetrahydrofolate interconversion / regulation of aerobic respiration / amino acid binding / mitochondrial nucleoid / RHOG GTPase cycle / Mitochondrial protein degradation / protein tetramerization / microtubule cytoskeleton / pyridoxal phosphate binding / one-carbon metabolic process / protein homotetramerization / mitochondrial inner membrane / mitochondrial matrix / chromatin binding / positive regulation of cell population proliferation / mitochondrion / extracellular exosome / identical protein binding / nucleus / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Rutkiewicz M / Tran LH / Ruszkowski M | |||||||||
Funding support | Poland, 1 items
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Citation | Journal: Acta Crystallogr D Struct Biol / Year: 2019 Title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty ...Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams / Abstract: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_18436.map.gz | 97.1 MB | EMDB map data format | |
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Header (meta data) | emd-18436-v30.xml emd-18436.xml | 18.8 KB 18.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_18436_fsc.xml | 9.9 KB | Display | FSC data file |
Images | emd_18436.png | 145 KB | ||
Filedesc metadata | emd-18436.cif.gz | 6.8 KB | ||
Others | emd_18436_half_map_1.map.gz emd_18436_half_map_2.map.gz | 95.3 MB 95.3 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-18436 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-18436 | HTTPS FTP |
-Validation report
Summary document | emd_18436_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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Full document | emd_18436_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | emd_18436_validation.xml.gz | 18.4 KB | Display | |
Data in CIF | emd_18436_validation.cif.gz | 23.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18436 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18436 | HTTPS FTP |
-Related structure data
Related structure data | 8qi7MC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_18436.map.gz / Format: CCP4 / Size: 103 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: 0.86 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_18436_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_18436_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : SHMT2 in the form of PLP internal aldimine
Entire | Name: SHMT2 in the form of PLP internal aldimine |
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Components |
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-Supramolecule #1: SHMT2 in the form of PLP internal aldimine
Supramolecule | Name: SHMT2 in the form of PLP internal aldimine / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Serine hydroxymethyltransferase, mitochondrial
Macromolecule | Name: Serine hydroxymethyltransferase, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: glycine hydroxymethyltransferase |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 52.944973 KDa |
Recombinant expression | Organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) |
Sequence | String: SNAAQTQTGE ANRGWTGQES LSDSDPEMWE LLQREKDRQC RGLELIASEN FCSRAALEAL GSCLNNKYSE GYPGKRYYGG AEVVDEIEL LCQRRALEAF DLDPAQWGVN VQPYSGSPAN LAVYTALLQP HDRIMGLDLP DGGHLTHGYM SDVKRISATS I FFESMPYK ...String: SNAAQTQTGE ANRGWTGQES LSDSDPEMWE LLQREKDRQC RGLELIASEN FCSRAALEAL GSCLNNKYSE GYPGKRYYGG AEVVDEIEL LCQRRALEAF DLDPAQWGVN VQPYSGSPAN LAVYTALLQP HDRIMGLDLP DGGHLTHGYM SDVKRISATS I FFESMPYK LNPKTGLIDY NQLALTARLF RPRLIIAGTS AYARLIDYAR MREVCDEVKA HLLADMAHIS GLVAAKVIPS PF KHADIVT TTTH(LLP)TLRGA RSGLIFYRKG VKAVDPKTGR EIPYTFEDRI NFAVFPSLQG GPHNHAIAAV AVALKQACT PMFREYSLQV LKNARAMADA LLERGYSLVS GGTDNHLVLV DLRPKGLDGA RAERVLELVS ITANKNTCPG DRSAITPGGL RLGAPALTS RQFREDDFRR VVDFIDEGVN IGLEVKSKTA KLQDFKSFLL KDSETSQRLA NLRQRVEQFA RAFPMPGFDE H UniProtKB: Serine hydroxymethyltransferase, mitochondrial |
-Macromolecule #2: water
Macromolecule | Name: water / type: ligand / ID: 2 / Number of copies: 117 / 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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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.6 mg/mL |
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Buffer | pH: 7.5 / Details: 25 mM Hepes pH 7.5, 150 mM NaCl, 1 mM TCEP |
Grid | Material: COPPER / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 1 / Number real images: 7948 / Average electron dose: 40.4 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |