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- EMDB-16973: DNA-unbound MutSbeta-ATP complex (bent clamp form) -

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Basic information

Entry
Database: EMDB / ID: EMD-16973
TitleDNA-unbound MutSbeta-ATP complex (bent clamp form)
Map dataDNA-unbound MutSbeta-ATP complex (bent clamp form)
Sample
  • Complex: DNA-unbound MutSbeta-ATP complex (bent clamp form)
    • Protein or peptide: DNA mismatch repair protein Msh2
    • Protein or peptide: DNA mismatch repair protein Msh3
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
KeywordsDNA repair protein complex / DNA BINDING PROTEIN
Function / homology
Function and homology information


somatic recombination of immunoglobulin genes involved in immune response / MutSbeta complex / Defective Mismatch Repair Associated With MSH3 / MutSalpha complex / Defective Mismatch Repair Associated With MSH2 / Defective Mismatch Repair Associated With MSH6 / guanine/thymine mispair binding / somatic recombination of immunoglobulin gene segments / B cell mediated immunity / maintenance of DNA repeat elements ...somatic recombination of immunoglobulin genes involved in immune response / MutSbeta complex / Defective Mismatch Repair Associated With MSH3 / MutSalpha complex / Defective Mismatch Repair Associated With MSH2 / Defective Mismatch Repair Associated With MSH6 / guanine/thymine mispair binding / somatic recombination of immunoglobulin gene segments / B cell mediated immunity / maintenance of DNA repeat elements / positive regulation of helicase activity / positive regulation of isotype switching to IgA isotypes / centromeric DNA binding / mitotic recombination / positive regulation of isotype switching to IgG isotypes / mismatched DNA binding / negative regulation of DNA recombination / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / isotype switching / oxidative phosphorylation / response to UV-B / postreplication repair / mitotic intra-S DNA damage checkpoint signaling / ATP-dependent DNA damage sensor activity / germ cell development / response to X-ray / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / somatic hypermutation of immunoglobulin genes / mismatch repair / ATP-dependent activity, acting on DNA / protein localization to chromatin / B cell differentiation / determination of adult lifespan / TP53 Regulates Transcription of DNA Repair Genes / male gonad development / double-strand break repair / double-stranded DNA binding / in utero embryonic development / negative regulation of neuron apoptotic process / damaged DNA binding / chromosome, telomeric region / DNA repair / chromatin binding / enzyme binding / protein homodimerization activity / ATP hydrolysis activity / DNA binding / nucleoplasm / ATP binding / membrane / nucleus
Similarity search - Function
DNA mismatch repair Msh2-type / DNA mismatch repair protein Msh2 / DNA mismatch repair protein MutS-like, N-terminal / DNA mismatch repair protein MutS, connector domain / DNA mismatch repair protein MutS, clamp / DNA mismatch repair protein MutS, N-terminal / MutS, connector domain superfamily / MutS domain I / MutS domain II / MutS family domain IV ...DNA mismatch repair Msh2-type / DNA mismatch repair protein Msh2 / DNA mismatch repair protein MutS-like, N-terminal / DNA mismatch repair protein MutS, connector domain / DNA mismatch repair protein MutS, clamp / DNA mismatch repair protein MutS, N-terminal / MutS, connector domain superfamily / MutS domain I / MutS domain II / MutS family domain IV / MutS domain III / DNA mismatch repair MutS family / DNA mismatch repair protein MutS, C-terminal / DNA mismatch repair protein MutS, core / DNA mismatch repair protein MutS, core domain superfamily / MutS domain V / DNA mismatch repair proteins mutS family signature. / DNA-binding domain of DNA mismatch repair MUTS family / ATPase domain of DNA mismatch repair MUTS family / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
DNA mismatch repair protein Msh3 / DNA mismatch repair protein Msh2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.43 Å
AuthorsLee J-H / Thomsen M / Daub H / Steinbacher S / Sztyler A / Thieulin-Pardo G / Neudegger T / Plotnikov N / Iyer RR / Wilkinson H ...Lee J-H / Thomsen M / Daub H / Steinbacher S / Sztyler A / Thieulin-Pardo G / Neudegger T / Plotnikov N / Iyer RR / Wilkinson H / Monteagudo E / Felsenfeld DP / Haque T / Finley M / Dominguez C / Vogt TF / Prasad BC
Funding support United States, 1 items
OrganizationGrant numberCountry
CHDI Foundation United States
CitationJournal: To Be Published
Title: DNA-unbound MutSbeta-ATP complex (bent clamp form)
Authors: Lee J-H / Thomsen M / Daub H / Steinbacher S / Sztyler A / Thieulin-Pardo G / Neudegger T / Plotnikov N / Iyer RR / Wilkinson H / Monteagudo E / Felsenfeld DP / Haque T / Finley M / ...Authors: Lee J-H / Thomsen M / Daub H / Steinbacher S / Sztyler A / Thieulin-Pardo G / Neudegger T / Plotnikov N / Iyer RR / Wilkinson H / Monteagudo E / Felsenfeld DP / Haque T / Finley M / Dominguez C / Vogt TF / Prasad BC
History
DepositionMar 31, 2023-
Header (metadata) releaseMay 24, 2023-
Map releaseMay 24, 2023-
UpdateJul 24, 2024-
Current statusJul 24, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_16973.png

Downloads & links

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Map

FileDownload / File: emd_16973.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationDNA-unbound MutSbeta-ATP complex (bent clamp form)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.91 Å/pix.
x 320 pix.
= 292.544 Å		0.91 Å/pix.
x 320 pix.
= 292.544 Å		0.91 Å/pix.
x 320 pix.
= 292.544 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.9142 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.02
Minimum - Maximum-0.0017054507 - 1.9759109
Average (Standard dev.)0.0008413048 (±0.021592656)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 292.544 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: DNA-unbound MutSbeta-ATP complex (bent clamp form)

Fileemd_16973_half_map_1.map
AnnotationDNA-unbound MutSbeta-ATP complex (bent clamp form)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: DNA-unbound MutSbeta-ATP complex (bent clamp form)

Fileemd_16973_half_map_2.map
AnnotationDNA-unbound MutSbeta-ATP complex (bent clamp form)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : DNA-unbound MutSbeta-ATP complex (bent clamp form)

EntireName: DNA-unbound MutSbeta-ATP complex (bent clamp form)
Components
  • Complex: DNA-unbound MutSbeta-ATP complex (bent clamp form)
    • Protein or peptide: DNA mismatch repair protein Msh2
    • Protein or peptide: DNA mismatch repair protein Msh3
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION

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Supramolecule #1: DNA-unbound MutSbeta-ATP complex (bent clamp form)

SupramoleculeName: DNA-unbound MutSbeta-ATP complex (bent clamp form) / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: DNA mismatch repair protein Msh2

MacromoleculeName: DNA mismatch repair protein Msh2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 104.861875 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MAVQPKETLQ LESAAEVGFV RFFQGMPEKP TTTVRLFDRG DFYTAHGEDA LLAAREVFKT QGVIKYMGPA GAKNLQSVVL SKMNFESFV KDLLLVRQYR VEVYKNRAGN KASKENDWYL AYKASPGNLS QFEDILFGNN DMSASIGVVG VKMSAVDGQR Q VGVGYVDS ...String:
MAVQPKETLQ LESAAEVGFV RFFQGMPEKP TTTVRLFDRG DFYTAHGEDA LLAAREVFKT QGVIKYMGPA GAKNLQSVVL SKMNFESFV KDLLLVRQYR VEVYKNRAGN KASKENDWYL AYKASPGNLS QFEDILFGNN DMSASIGVVG VKMSAVDGQR Q VGVGYVDS IQRKLGLCEF PDNDQFSNLE ALLIQIGPKE CVLPGGETAG DMGKLRQIIQ RGGILITERK KADFSTKDIY QD LNRLLKG KKGEQMNSAV LPEMENQVAV SSLSAVIKFL ELLSDDSNFG QFELTTFDFS QYMKLDIAAV RALNLFQGSV EDT TGSQSL AALLNKCKTP QGQRLVNQWI KQPLMDKNRI EERLNLVEAF VEDAELRQTL QEDLLRRFPD LNRLAKKFQR QAAN LQDCY RLYQGINQLP NVIQALEKHE GKHQKLLLAV FVTPLTDLRS DFSKFQEMIE TTLDMDQVEN HEFLVKPSFD PNLSE LREI MNDLEKKMQS TLISAARDLG LDPGKQIKLD SSAQFGYYFR VTCKEEKVLR NNKNFSTVDI QKNGVKFTNS KLTSLN EEY TKNKTEYEEA QDAIVKEIVN ISSGYVEPMQ TLNDVLAQLD AVVSFAHVSN GAPVPYVRPA ILEKGQGRII LKASRHA CV EVQDEIAFIP NDVYFEKDKQ MFHIITGPNM GGKSTYIRQT GVIVLMAQIG CFVPCESAEV SIVDCILARV GAGDSQLK G VSTFMAEMLE TASILRSATK DSLIIIDELG RGTSTYDGFG LAWAISEYIA TKIGAFCMFA THFHELTALA NQIPTVNNL HVTALTTEET LTMLYQVKKG VCDQSFGIHV AELANFPKHV IECAKQKALE LEEFQYIGES QGYDIMEPAA KKCYLEREQG EKIIQEFLS KVKQMPFTEM SEENITIKLK QLKAEVIAKN NSFVNEIISR IKVTT

UniProtKB: DNA mismatch repair protein Msh2

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Macromolecule #2: DNA mismatch repair protein Msh3

MacromoleculeName: DNA mismatch repair protein Msh3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 127.618703 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MSRRKPASGG LAASSSAPAR QAVLSRFFQS TGSLKSTSSS TGAADQVDPG AAAAAAAAAA AAPPAPPAPA FPPQLPPHIA TEIDRRKKR PLENDGPVKK KVKKVQQKEG GSDLGMSGNS EPKKCLRTRN VSKSLEKLKE FCCDSALPQS RVQTESLQER F AVLPKCTD ...String:
MSRRKPASGG LAASSSAPAR QAVLSRFFQS TGSLKSTSSS TGAADQVDPG AAAAAAAAAA AAPPAPPAPA FPPQLPPHIA TEIDRRKKR PLENDGPVKK KVKKVQQKEG GSDLGMSGNS EPKKCLRTRN VSKSLEKLKE FCCDSALPQS RVQTESLQER F AVLPKCTD FDDISLLHAK NAVSSEDSKR QINQKDTTLF DLSQFGSSNT SHENLQKTAS KSANKRSKSI YTPLELQYIE MK QQHKDAV LCVECGYKYR FFGEDAEIAA RELNIYCHLD HNFMTASIPT HRLFVHVRRL VAKGYKVGVV KQTETAALKA IGD NRSSLF SRKLTALYTK STLIGEDVNP LIKLDDAVNV DEIMTDTSTS YLLCISENKE NVRDKKKGNI FIGIVGVQPA TGEV VFDSF QDSASRSELE TRMSSLQPVE LLLPSALSEQ TEALIHRATS VSVQDDRIRV ERMDNIYFEY SHAFQAVTEF YAKDT VDIK GSQIISGIVN LEKPVICSLA AIIKYLKEFN LEKMLSKPEN FKQLSSKMEF MTINGTTLRN LEILQNQTDM KTKGSL LWV LDHTKTSFGR RKLKKWVTQP LLKLREINAR LDAVSEVLHS ESSVFGQIEN HLRKLPDIER GLCSIYHKKC STQEFFL IV KTLYHLKSEF QAIIPAVNSH IQSDLLRTVI LEIPELLSPV EHYLKILNEQ AAKVGDKTEL FKDLSDFPLI KKRKDEIQ G VIDEIRMHLQ EIRKILKNPS AQYVTVSGQE FMIEIKNSAV SCIPTDWVKV GSTKAVSRFH SPFIVENYRH LNQLREQLV LDCSAEWLDF LEKFSEHYHS LCKAVHHLAT VDCIFSLAKV AKQGDYCRPT VQEERKIVIK NGRHPVIDVL LGEQDQYVPN NTDLSEDSE RVMIITGPNM GGKSSYIKQV ALITIMAQIG SYVPAEEATI GIVDGIFTRM GAADNIYKGR STFMEELTDT A EIIRKATS QSLVILDELG RGTSTHDGIA IAYATLEYFI RDVKSLTLFV THYPPVCELE KNYSHQVGNY HMGFLVSEDE SK LDPGAAE QVPDFVTFLY QITRGIAARS YGLNVAKLAD VPGEILKKAA HKSKELEGLI NTKRKRLKYF AKLWTMHNAQ DLQ KWTEEF NMEETQTSLL H

UniProtKB: DNA mismatch repair protein Msh3

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Macromolecule #3: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 2 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #4: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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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

BufferpH: 7.5
VitrificationCryogen name: ETHANE-PROPANE

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 57.38 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.7000000000000001 µm

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

3thz

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.43 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 263343
Initial angle assignmentType: OTHER
Final angle assignmentType: MAXIMUM LIKELIHOOD

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