[English] 日本語
Yorodumi
- PDB-9kfe: Truncated Fzo1 with modified LD, GTP-bound -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9kfe
TitleTruncated Fzo1 with modified LD, GTP-bound
ComponentsMitofusin FZO1,Mitofusin FZO1,Fzo1
KeywordsHYDROLASE / Fzo1 / dynamin / mitofusin
Function / homology
Function and homology information


peroxisomal-mitochondrial contact site / peroxisome-mitochondrion membrane tether activity / mitochondrial outer membrane fusion / Factors involved in megakaryocyte development and platelet production / RHOT2 GTPase cycle / mitochondrial inner membrane fusion / PINK1-PRKN Mediated Mitophagy / mitochondrion localization / mitochondrial fusion / intracellular distribution of mitochondria ...peroxisomal-mitochondrial contact site / peroxisome-mitochondrion membrane tether activity / mitochondrial outer membrane fusion / Factors involved in megakaryocyte development and platelet production / RHOT2 GTPase cycle / mitochondrial inner membrane fusion / PINK1-PRKN Mediated Mitophagy / mitochondrion localization / mitochondrial fusion / intracellular distribution of mitochondria / mitochondrial membrane / peroxisome / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / mitochondrial outer membrane / GTPase activity / GTP binding / mitochondrion
Similarity search - Function
Mitofusin family / Dynamin-type guanine nucleotide-binding (G) domain / Dynamin-type guanine nucleotide-binding (G) domain profile. / Dynamin, N-terminal / Dynamin family / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
GUANOSINE-5'-TRIPHOSPHATE / : / Mitofusin FZO1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.81 Å
AuthorsGao, S. / Huang, S.-J.
Funding support China, 2items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)2320103002 China
National Natural Science Foundation of China (NSFC)82173098 China
CitationJournal: To Be Published
Title: A special latch in yeast mitofusin guarantees mitochondrial fusion by stabilizing self-assembly
Authors: Gao, S. / Huang, S.J.
History
DepositionNov 6, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 27, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Mitofusin FZO1,Mitofusin FZO1,Fzo1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,8174
Polymers54,2301
Non-polymers5873
Water181
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: light scattering
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area910 Å2
ΔGint-13 kcal/mol
Surface area18600 Å2
MethodPISA
Unit cell
Length a, b, c (Å)77.133, 77.133, 284.664
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number179
Space group name H-MP6522
Space group name HallP652(x,y,z+1/12)
Symmetry operation#1: x,y,z
#2: x-y,x,z+5/6
#3: y,-x+y,z+1/6
#4: -y,x-y,z+2/3
#5: -x+y,-x,z+1/3
#6: x-y,-y,-z
#7: -x,-x+y,-z+1/3
#8: -x,-y,z+1/2
#9: y,x,-z+2/3
#10: -y,-x,-z+1/6
#11: -x+y,y,-z+1/2
#12: x,x-y,-z+5/6
Components on special symmetry positions
IDModelComponents
11A-90-

TRP

-
Components

#1: Protein Mitofusin FZO1,Mitofusin FZO1,Fzo1 / Transmembrane GTPase FZO1


Mass: 54230.426 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: FZO1, YBR179C, YBR1241 / Production host: Escherichia coli (E. coli)
References: UniProt: P38297, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement
#2: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: GTP, energy-carrying molecule*YM
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.25 Å3/Da / Density % sol: 45.43 %
Crystal growTemperature: 277.15 K / Method: vapor diffusion, hanging drop / Details: 150mM Cesium chloride, 17% PEG3350

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL02U1 / Wavelength: 0.979183 Å
DetectorType: DECTRIS EIGER2 S 9M / Detector: PIXEL / Date: Sep 22, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979183 Å / Relative weight: 1
ReflectionResolution: 2.81→48.7 Å / Num. obs: 12840 / % possible obs: 98.6 % / Redundancy: 5 % / CC1/2: 0.991 / Rmerge(I) obs: 0.128 / Rpim(I) all: 0.083 / Rrim(I) all: 0.154 / Net I/σ(I): 9.8
Reflection shellResolution: 2.81→2.97 Å / Rmerge(I) obs: 0.196 / Mean I/σ(I) obs: 6.5 / Num. unique obs: 1775 / CC1/2: 0.787 / Rpim(I) all: 0.128 / Rrim(I) all: 0.236

-
Processing

Software
NameVersionClassification
PHENIX1.19_4092refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.81→38.22 Å / SU ML: 0.349 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 22.2918
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2672 1259 10.01 %
Rwork0.2188 11320 -
obs0.2237 12579 96.43 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 20.97 Å2
Refinement stepCycle: LAST / Resolution: 2.81→38.22 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3114 0 34 1 3149
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00173207
X-RAY DIFFRACTIONf_angle_d0.47044328
X-RAY DIFFRACTIONf_chiral_restr0.0371506
X-RAY DIFFRACTIONf_plane_restr0.0032542
X-RAY DIFFRACTIONf_dihedral_angle_d4.1174412
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.81-2.930.33921310.28431181X-RAY DIFFRACTION93.58
2.93-3.060.3281400.2731258X-RAY DIFFRACTION99.57
3.06-3.220.30631410.25311275X-RAY DIFFRACTION99.79
3.22-3.420.29281390.22461245X-RAY DIFFRACTION99.64
3.42-3.690.23881430.20841290X-RAY DIFFRACTION99.51
3.69-4.060.27241430.19261284X-RAY DIFFRACTION99.44
4.06-4.640.20591420.16531282X-RAY DIFFRACTION98.75
4.64-5.840.25141360.20961207X-RAY DIFFRACTION90.07
5.85-38.220.22881440.20541298X-RAY DIFFRACTION88.96
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.97690781740.791831191171-0.2299583026341.70149676530.2706470322421.91457736447-0.2111227587120.1363386958850.423899128464-0.4582807223740.04997026057460.0201023667974-0.260127025998-0.1136639490120.1223858045980.275974685056-0.0688467860802-0.0966948736230.05494896943510.03705991607440.150097483258-21.4587160737-21.806713078110.9123656913
20.5191112581370.2939309899350.3486783942481.155753921660.4500956266481.25625196519-0.03554117943140.0593816923802-0.108073057599-0.0821818264339-0.078856866691-0.03492169145570.1483705211530.1076110568580.02342286648830.1012460268660.03213509386010.04465533589090.005941918221-0.001497727430680.09020747456331.4652867916-19.0763701729-2.67630924852
31.862628605770.38931186253-0.05520499902360.9489438736260.06278044863540.6962107100920.0372807240602-0.2878035438880.09067839420940.155891775206-0.0834685416807-0.101242960090.01952889811160.09926305777170.1818671237750.1473691572670.0500077427841-0.08570990106710.03543802957230.04972665977420.0398389922409-6.37200962082-16.637020408415.9601968371
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Auth asym-ID: A / Label asym-ID: A

IDRefine TLS-IDSelection detailsAuth seq-IDLabel seq-ID
11chain 'A' and (resid 84 through 184 )84 - 1841 - 75
22chain 'A' and (resid 185 through 377 )185 - 37776 - 266
33chain 'A' and (resid 378 through 854 )378 - 854267 - 388

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more