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- EMDB-18436: Cryo-EM Structure of Human Serine Hydroxymethyltransferase, isofo... -

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Basic information

Entry
Database: EMDB / ID: EMD-18436
TitleCryo-EM Structure of Human Serine Hydroxymethyltransferase, isoform 2 (SHMT2)
Map data
Sample
  • Complex: SHMT2 in the form of PLP internal aldimineSerine hydroxymethyltransferase
    • Protein or peptide: Serine hydroxymethyltransferase, mitochondrial
  • Ligand: water
Keywordsone-carbon metabolism / folate cycle / tetrahydtofolate / mitochondria / TRANSFERASE
Function / homology
Function and homology information


BRISC complex / L-allo-threonine aldolase activity / regulation of mitochondrial translation / purine nucleobase biosynthetic process / serine binding / L-serine catabolic process / L-serine metabolic process / glycine metabolic process / L-serine biosynthetic process / glycine hydroxymethyltransferase ...BRISC complex / L-allo-threonine aldolase activity / regulation of mitochondrial translation / purine nucleobase biosynthetic process / serine binding / L-serine catabolic process / 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 / folic acid metabolic process / mitochondrial nucleoid / RHOG GTPase cycle / mRNA regulatory element binding translation repressor activity / protein tetramerization / mRNA 5'-UTR binding / microtubule cytoskeleton / pyridoxal phosphate binding / one-carbon metabolic process / protein homotetramerization / mitochondrial inner membrane / mitochondrial matrix / chromatin binding / positive regulation of cell population proliferation / protein homodimerization activity / mitochondrion / extracellular exosome / zinc ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Serine hydroxymethyltransferase, pyridoxal phosphate binding site / Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. / Serine hydroxymethyltransferase / Serine hydroxymethyltransferase-like domain / Serine hydroxymethyltransferase / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase
Similarity search - Domain/homology
Serine hydroxymethyltransferase, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsRutkiewicz M / Tran LH / Ruszkowski M
Funding support Poland, 1 items
OrganizationGrant numberCountry
Other government Poland
CitationJournal: 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
DepositionSep 11, 2023-
Header (metadata) releaseSep 20, 2023-
Map releaseSep 20, 2023-
UpdateNov 15, 2023-
Current statusNov 15, 2023Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_18436.png

Downloads & links

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Map

FileDownload / File: emd_18436.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.86 Å
Density
Contour LevelBy AUTHOR: 0.19
Minimum - Maximum-0.70370305 - 1.1261568
Average (Standard dev.)0.00061813573 (±0.04481805)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 258.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_18436_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_18436_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : SHMT2 in the form of PLP internal aldimine

EntireName: SHMT2 in the form of PLP internal aldimineSerine hydroxymethyltransferase
Components
  • Complex: SHMT2 in the form of PLP internal aldimineSerine hydroxymethyltransferase
    • Protein or peptide: Serine hydroxymethyltransferase, mitochondrial
  • Ligand: water

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Supramolecule #1: SHMT2 in the form of PLP internal aldimine

SupramoleculeName: SHMT2 in the form of PLP internal aldimine / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Serine hydroxymethyltransferase, mitochondrial

MacromoleculeName: Serine hydroxymethyltransferase, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: glycine hydroxymethyltransferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 52.944973 KDa
Recombinant expressionOrganism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
SequenceString: 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

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Macromolecule #2: water

MacromoleculeName: water / type: ligand / ID: 2 / Number of copies: 117 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER / Water

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.6 mg/mL
BufferpH: 7.5 / Details: 25 mM Hepes pH 7.5, 150 mM NaCl, 1 mM TCEP
GridMaterial: COPPER / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm
Image recordingFilm 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
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.0.3)
Final 3D classificationNumber classes: 100 / Software - Name: cryoSPARC (ver. 4.0.3)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.0.3)
Final reconstructionNumber classes used: 29 / Applied symmetry - Point group: D2 (2x2 fold dihedral) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.0.3) / Number images used: 146577
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

8aql


Chain - Chain ID: A / Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-8qi7:
Cryo-EM Structure of Human Serine Hydroxymethyltransferase, isoform 2 (SHMT2)

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