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- EMDB-8772: Core Factor local refinement from Pol I Initial Transcribing Comp... -

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Basic information

Entry
Database: EMDB / ID: EMD-8772
TitleCore Factor local refinement from Pol I Initial Transcribing Complex at 4.2 angstrom
Map dataCore Factor local refinement from Pol I Initial Transcribing Complex
Sample
  • Complex: Yeast Core Factor
    • Protein or peptide: Rrn7
    • Protein or peptide: Rrn11
    • Protein or peptide: Rrn6
    • DNA: non-template strand DNA
    • DNA: template DNA
Function / homology
Function and homology information


RNA polymerase I transcription regulatory region sequence-specific DNA binding / RNA polymerase I core factor complex / RNA polymerase I general transcription initiation factor activity / RNA polymerase I general transcription initiation factor binding / RNA polymerase I core promoter sequence-specific DNA binding / RNA Polymerase I Promoter Escape / nucleolar large rRNA transcription by RNA polymerase I / transcription initiation at RNA polymerase I promoter / TBP-class protein binding / nucleolus ...RNA polymerase I transcription regulatory region sequence-specific DNA binding / RNA polymerase I core factor complex / RNA polymerase I general transcription initiation factor activity / RNA polymerase I general transcription initiation factor binding / RNA polymerase I core promoter sequence-specific DNA binding / RNA Polymerase I Promoter Escape / nucleolar large rRNA transcription by RNA polymerase I / transcription initiation at RNA polymerase I promoter / TBP-class protein binding / nucleolus / zinc ion binding / nucleus / cytoplasm
Similarity search - Function
Transcription initiation factor Rrn11 / RNA polymerase I-specific transcription initiation factor Rrn6 / Transcription initiation factor Rrn11, budding yeast / RNA polymerase I-specific transcription initiation factor RRN6-like / : / : / : / : / RNA polymerase I-specific transcription initiation factor Rrn11 / Rrn6, beta-propeller ...Transcription initiation factor Rrn11 / RNA polymerase I-specific transcription initiation factor Rrn6 / Transcription initiation factor Rrn11, budding yeast / RNA polymerase I-specific transcription initiation factor RRN6-like / : / : / : / : / RNA polymerase I-specific transcription initiation factor Rrn11 / Rrn6, beta-propeller / RRN6, K-rich C-terminal domain / Rrn6, helical bundle domain / Transcription initiation factor Rrn7, Zinc-finger / RNA polymerase I transcription initiation factor TAF1B/Rrn7 / : / : / Zinc-finger of RNA-polymerase I-specific TFIIB, Rrn7 / Rrn7/TAF1B, N-terminal cyclin domain / Rrn7/TAF1B, C-terminal cyclin domain
Similarity search - Domain/homology
RNA polymerase I-specific transcription initiation factor RRN6 / RNA polymerase I-specific transcription initiation factor RRN7 / RNA polymerase I-specific transcription initiation factor RRN11
Similarity search - Component
Biological speciesSaccharomyces cerevisiae S288c (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsHan Y / He Y
Funding support United States, 5 items
OrganizationGrant numberCountry
Northwestern UniversityCornew Innovation Award United States
National Institutes of Health/National Cancer Institute (NIH/NCI)NCI 5K22CA184235 United States
American Cancer SocietyIRG-15-173-21 United States
National Science Foundation (NSF, United States)MCB-1149521 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)NIGMS GM110387 United States
CitationJournal: Elife / Year: 2017
Title: Structural mechanism of ATP-independent transcription initiation by RNA polymerase I.
Authors: Yan Han / Chunli Yan / Thi Hoang Duong Nguyen / Ashleigh J Jackobel / Ivaylo Ivanov / Bruce A Knutson / Yuan He /
Abstract: Transcription initiation by RNA Polymerase I (Pol I) depends on the Core Factor (CF) complex to recognize the upstream promoter and assemble into a Pre-Initiation Complex (PIC). Here, we solve a ...Transcription initiation by RNA Polymerase I (Pol I) depends on the Core Factor (CF) complex to recognize the upstream promoter and assemble into a Pre-Initiation Complex (PIC). Here, we solve a structure of Pol I-CF-DNA to 3.8 Å resolution using single-particle cryo-electron microscopy. The structure reveals a bipartite architecture of Core Factor and its recognition of the promoter from -27 to -16. Core Factor's intrinsic mobility correlates well with different conformational states of the Pol I cleft, in addition to the stabilization of either Rrn7 N-terminal domain near Pol I wall or the tandem winged helix domain of A49 at a partially overlapping location. Comparison of the three states in this study with the Pol II system suggests that a ratchet motion of the Core Factor-DNA sub-complex at upstream facilitates promoter melting in an ATP-independent manner, distinct from a DNA translocase actively threading the downstream DNA in the Pol II PIC.
History
DepositionJun 16, 2017-
Header (metadata) releaseJul 5, 2017-
Map releaseJul 5, 2017-
UpdateDec 25, 2019-
Current statusDec 25, 2019Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.07
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.07
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_8772.png

Downloads & links

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Map

FileDownload / File: emd_8772.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCore Factor local refinement from Pol I Initial Transcribing Complex
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.3 Å/pix.
x 192 pix.
= 249.6 Å		1.3 Å/pix.
x 192 pix.
= 249.6 Å		1.3 Å/pix.
x 192 pix.
= 249.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.3 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.07 / Movie #1: 0.07
Minimum - Maximum-0.27590472 - 0.39845526
Average (Standard dev.)0.0007010981 (±0.010016483)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions192192192
Spacing192192192
CellA=B=C: 249.59999 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.31.31.3
M x/y/z192192192
origin x/y/z0.0000.0000.000
length x/y/z249.600249.600249.600
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ281156
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS192192192
D min/max/mean-0.2760.3980.001

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Supplemental data

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Sample components

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Entire : Yeast Core Factor

EntireName: Yeast Core Factor
Components
  • Complex: Yeast Core Factor
    • Protein or peptide: Rrn7
    • Protein or peptide: Rrn11
    • Protein or peptide: Rrn6
    • DNA: non-template strand DNA
    • DNA: template DNA

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Supramolecule #1: Yeast Core Factor

SupramoleculeName: Yeast Core Factor / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Saccharomyces cerevisiae S288c (yeast)
Molecular weightTheoretical: 250 KDa

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Macromolecule #1: Rrn7

MacromoleculeName: Rrn7 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288c (yeast)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSTFIRGPIC GTDNCPSRLW RIIDGRRTCQ YGHVMEGDVE FNDDEDDLNG LGAGVITRRL NLTTNATGS FQSSQLTNSQ LLQQQQRQSH KKFKKLIGHE AKLLFLKSFQ FILKRQIRWL I TEMRFPKE FEHVAKIIWL KILKTINDQP QEELKLQLHM TSTISILYLA ...String:
MSTFIRGPIC GTDNCPSRLW RIIDGRRTCQ YGHVMEGDVE FNDDEDDLNG LGAGVITRRL NLTTNATGS FQSSQLTNSQ LLQQQQRQSH KKFKKLIGHE AKLLFLKSFQ FILKRQIRWL I TEMRFPKE FEHVAKIIWL KILKTINDQP QEELKLQLHM TSTISILYLA STHLSLPVYT CD YIKWICT AKMPYFQASE ILPKSWRIQL PNYYVSILEG SISPFNGQLY NKIALTCGMI HFK EFFNSE ISCQGLLLKL VMQCALPPEF YFYTKQVIEF EETDIRNLTL WERTDERHTG RVSN HAELR VLSYFMLTIN WMLSFDRDRQ YPLKWILSLT ESLTQRTTTS ESIGRNIVKV VYPDK PTSS DYFQWSEEET LEFLKWMEKQ FLPTQTKSLH NENGSMEMTI DQKIARRKLY KIFPLD REA NHDGEFNDST HQLTFIEDLQ ERYAKQTPFF ESNKIRDSLN YQEANPPARK EAIGRLL TH IASQLLVDFA ISKEQLKDCI SRIKNACLHR MN

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Macromolecule #2: Rrn11

MacromoleculeName: Rrn11 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288c (yeast)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MFEVPITLTN RKFAQRRKLK YQYINYISRR FDRISKKSTT TDSLPTPENS AAENNDEEEG QNSEAGTYR RSVLQQKKRR RERHWRSVVG EIYSTTESET DSQEEETEEG GEHDTGIDKE D SDEERKFW KKYEKPEKSF EIWRTVSSQN KQPINKQKMT YHNFKKIEKI ...String:
MFEVPITLTN RKFAQRRKLK YQYINYISRR FDRISKKSTT TDSLPTPENS AAENNDEEEG QNSEAGTYR RSVLQQKKRR RERHWRSVVG EIYSTTESET DSQEEETEEG GEHDTGIDKE D SDEERKFW KKYEKPEKSF EIWRTVSSQN KQPINKQKMT YHNFKKIEKI PLRKMEIPLL HC TKENKLY FQSISRGLEP LKTSTSEVRN YRTRHIVTLT DLLHLNVSRH NWSLAYKIFA TLI RIPGVQ IKSLWGIGVE ILDNLSNSSS GLDFLQWMCQ IYSSKSRFVQ NINYRSIVPP FQTG SRTHT AKFAITYLWS SLINCQKSME PSSNIIDKPF DTENDLLQEL IDKISEWVLT PPFME DAEV WFIYASCHLL KADTLSRQFV NDNKNNDLIG LDRDIKINQV IKHIHYVRTF LKICLD KGG FAVPSRLIEN QLKSFESRLY GEAQDIQERD VANVYDSIDN SSVENSFGDV YETNAEF LD TQLMDLSPED NGLDEMHYSD EDSSE

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Macromolecule #3: Rrn6

MacromoleculeName: Rrn6 / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288c (yeast)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSEGQIPSSD VLGSQLGVGV QGASLYCPQE NYTTKKQEKP QWLRPVDDTL AEDALDLHIV VKSLLCDTA IRYISDDKVL QESDADDDLI TSDIDEDTDN QGDTSIVVNP VIPVVPKDVH F FKKVDVGN DSMFGVNCDT PVSFQDYIPS DLLRNLDDTL QESTNSSRPM ...String:
MSEGQIPSSD VLGSQLGVGV QGASLYCPQE NYTTKKQEKP QWLRPVDDTL AEDALDLHIV VKSLLCDTA IRYISDDKVL QESDADDDLI TSDIDEDTDN QGDTSIVVNP VIPVVPKDVH F FKKVDVGN DSMFGVNCDT PVSFQDYIPS DLLRNLDDTL QESTNSSRPM QDAFFWDPTV AN RLDSQYI QTASDLRNYR DGTEIIAYAS GKTGSVLNIA VLTRQNTLHL NRHNNVTSIE LHS PIKSIK IPGASESIGR RSNLVGIITE NSFQIFRIES VHSRSCDVMV SSSEPLYFVE IDDL QVVDF AFNPWDLQQF AIIDIKGNWS IGRIPKNFNN NNKRKLQLID NLHGTIFDPE ELSSW KRIE WFSHFQKILV FDRSKMIEID FMNNWQTEVV QAKAWSNIRD YKRIDDKNGI LLTSRE III VGASESNDPV RRISWKHDLD PDDTTLRITV QKVKKPDHIL LVAFVYSMRH KRIYMHV FS HRKANLFQSL GCSTVLEIPG GTPTGIETIL TLDHIDDESR REEDADENFE LVVDFLVK L RNSSEVYYYA LSNTQNSEPN KQETPIIVDH PEWASLFNNA DEREKESIGA LVSQIKLKE RERISRVQNL IEHENSHDED KYLQDLGYRL SIATNELLES WQKTKDESIL SGSLSHSKLK NLLENSDSF ASIPEFSSLL DQFFQYYQDQ DVTFIGFEKL LHLFLHEDVP GLDIFYNKLL Q CWVLVSPQ AELLTKEIVK DIIWSLARLE KPSLFEPIQN EISRSLSGPY QDIISSWDMD DI NEEDESN EFNFDSQFSA PFNGRPPFNL NSQSQIPTIK SSQSSGLARR KRILKTQSQK ATP LSQSTQ NLSVLPDSMT PAFTLMQPPS SQISFVNDSQ PRNSQKAKKK KKRIRGFG

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Macromolecule #4: non-template strand DNA

MacromoleculeName: non-template strand DNA / type: dna / ID: 4 / Classification: DNA
Source (natural)Organism: Saccharomyces cerevisiae S288c (yeast)
SequenceString:
CAAGTGTGAG GAAAAGTAGT TGGGTTTTTT TTTTTTTTTT TGCAGTTGAA GACA

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Macromolecule #5: template DNA

MacromoleculeName: template DNA / type: dna / ID: 5 / Classification: DNA
Source (natural)Organism: Saccharomyces cerevisiae S288c (yeast)
SequenceString:
TGTCTTCAAC TGCTTTCGCA TGAAGTACCT CCCAACTACT TTTCCTCACA CTTG

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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: 7.6
GridModel: Quantifoil S7/2 / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average exposure time: 12.0 sec. / Average electron dose: 56.8 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated defocus max: 4.5 µm / Calibrated defocus min: 1.5 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal magnification: 22500
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: Gctf (ver. 0.5)
Details: CTF amplitude correction was performed following 3D auto refinement in relion.
Startup modelType of model: NONE / Details: This is a local refinement.
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.0) / Number images used: 124112
Initial angle assignmentType: RANDOM ASSIGNMENT / Software - Name: RELION (ver. 2.0)
Final angle assignmentType: PROJECTION MATCHING / Software - Name: RELION (ver. 2.0)
Final 3D classificationNumber classes: 5 / Software - Name: RELION (ver. 2.0)
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementProtocol: FLEXIBLE FIT

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