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Open data
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Basic information
Entry | Database: PDB / ID: 6agb | ||||||
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Title | Cryo-EM structure of yeast Ribonuclease P | ||||||
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![]() | HYDROLASE/RNA / Ribonuclease P / RNA-protein complex / HYDROLASE-RNA complex | ||||||
Function / homology | ![]() ribonuclease MRP activity / nuclear-transcribed mRNA catabolic process, RNase MRP-dependent / intronic box C/D snoRNA processing / nucleolar ribonuclease P complex / ribonuclease MRP complex / ribonuclease P RNA binding / ribonuclease P complex / ribonuclease P / ribonuclease P activity / rRNA primary transcript binding ...ribonuclease MRP activity / nuclear-transcribed mRNA catabolic process, RNase MRP-dependent / intronic box C/D snoRNA processing / nucleolar ribonuclease P complex / ribonuclease MRP complex / ribonuclease P RNA binding / ribonuclease P complex / ribonuclease P / ribonuclease P activity / rRNA primary transcript binding / tRNA 5'-leader removal / telomerase holoenzyme complex / tRNA processing / maturation of 5.8S rRNA / rRNA processing / RNA binding / nucleus / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.48 Å | ||||||
![]() | Lan, P. / Tan, M. / Wu, J. / Lei, M. | ||||||
![]() | ![]() Title: Structural insight into precursor tRNA processing by yeast ribonuclease P. Authors: Pengfei Lan / Ming Tan / Yuebin Zhang / Shuangshuang Niu / Juan Chen / Shaohua Shi / Shuwan Qiu / Xuejuan Wang / Xiangda Peng / Gang Cai / Hong Cheng / Jian Wu / Guohui Li / Ming Lei / ![]() Abstract: Ribonuclease P (RNase P) is a universal ribozyme responsible for processing the 5'-leader of pre-transfer RNA (pre-tRNA). Here, we report the 3.5-angstrom cryo-electron microscopy structures of ...Ribonuclease P (RNase P) is a universal ribozyme responsible for processing the 5'-leader of pre-transfer RNA (pre-tRNA). Here, we report the 3.5-angstrom cryo-electron microscopy structures of RNase P alone and in complex with pre-tRNA The protein components form a hook-shaped architecture that wraps around the RNA and stabilizes RNase P into a "measuring device" with two fixed anchors that recognize the L-shaped pre-tRNA. A universally conserved uridine nucleobase and phosphate backbone in the catalytic center together with the scissile phosphate and the O3' leaving group of pre-tRNA jointly coordinate two catalytic magnesium ions. Binding of pre-tRNA induces a conformational change in the catalytic center that is required for catalysis. Moreover, simulation analysis suggests a two-metal-ion S2 reaction pathway of pre-tRNA cleavage. These results not only reveal the architecture of yeast RNase P but also provide a molecular basis of how the 5'-leader of pre-tRNA is processed by eukaryotic RNase P. | ||||||
History |
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Structure visualization
Movie |
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 608.9 KB | Display | ![]() |
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PDB format | ![]() | 484.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 990.8 KB | Display | ![]() |
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Full document | ![]() | 1023.1 KB | Display | |
Data in XML | ![]() | 70 KB | Display | |
Data in CIF | ![]() | 110.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9616MC ![]() 9622C ![]() 6ah3C M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Ribonuclease P ... , 2 types, 2 molecules AK
#1: RNA chain | Mass: 118857.781 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell Source: (natural) ![]() ![]() Strain: ATCC 204508 / S288c / References: GenBank: 1163001456 |
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#10: Protein | Mass: 16375.049 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell Source: (natural) ![]() ![]() Strain: ATCC 204508 / S288c / References: UniProt: P40571, ribonuclease P |
-Ribonucleases P/MRP protein subunit ... , 5 types, 5 molecules BCFGH
#2: Protein | Mass: 100559.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell Source: (natural) ![]() ![]() Strain: ATCC 204508 / S288c / References: UniProt: P41812, ribonuclease P |
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#3: Protein | Mass: 22643.721 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell Source: (natural) ![]() ![]() Strain: ATCC 204508 / S288c / References: UniProt: P53833 |
#6: Protein | Mass: 18234.959 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell Source: (natural) ![]() ![]() Strain: ATCC 204508 / S288c / References: UniProt: P53218, ribonuclease P |
#7: Protein | Mass: 15844.284 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell Source: (natural) ![]() ![]() Strain: ATCC 204508 / S288c / References: UniProt: P38291, ribonuclease P |
#8: Protein | Mass: 15530.351 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell Source: (natural) ![]() ![]() Strain: ATCC 204508 / S288c / References: UniProt: P38208, ribonuclease P |
-Ribonuclease P/MRP protein subunit ... , 2 types, 3 molecules EIJ
#5: Protein | Mass: 19601.590 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell Source: (natural) ![]() ![]() Strain: ATCC 204508 / S288c / References: UniProt: P28005, ribonuclease P |
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#9: Protein | Mass: 32270.262 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell Source: (natural) ![]() ![]() Strain: ATCC 204508 / S288c / References: UniProt: P38786, ribonuclease P |
-Protein / Non-polymers , 2 types, 2 molecules D![](data/chem/img/ZN.gif)
![](data/chem/img/ZN.gif)
#11: Chemical | ChemComp-ZN / |
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#4: Protein | Mass: 32933.168 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: cell Source: (natural) ![]() ![]() Strain: ATCC 204508 / S288c / References: UniProt: P38336 |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: RNase P / Type: COMPLEX / Entity ID: #1-#10 / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: DIFFRACTION |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 3.48 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 164765 / Symmetry type: POINT |