[English] 日本語
Yorodumi
- PDB-8ud0: Sterile Alpha Motif (SAM) domain from Tric1 from Arabidopsis thal... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8ud0
TitleSterile Alpha Motif (SAM) domain from Tric1 from Arabidopsis thaliana - G241E mutant
ComponentsChloroplastic import inner membrane translocase subunit HP30-1
KeywordsRNA BINDING PROTEIN / Mitochondria / tRNA import / Tric1 / SAM domain / oligomerization / PRAT domain / sterile alpha motif domain
Function / homology
Function and homology information


tRNA import into mitochondrion / protein targeting to chloroplast / chloroplast inner membrane / protein insertion into mitochondrial inner membrane / chloroplast envelope / plastid / protein transmembrane transporter activity / mitochondrion organization / chloroplast / : ...tRNA import into mitochondrion / protein targeting to chloroplast / chloroplast inner membrane / protein insertion into mitochondrial inner membrane / chloroplast envelope / plastid / protein transmembrane transporter activity / mitochondrion organization / chloroplast / : / mitochondrion / cytosol
Similarity search - Function
Mitochondrial import inner membrane translocase subunit TIM22 / SAM domain (Sterile alpha motif) / Tim17/Tim22/Tim23/Pmp24 family / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily
Similarity search - Domain/homology
Chloroplastic import inner membrane translocase subunit HP30-1
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.89 Å
AuthorsOlasz, B. / Vrielink, A. / Smithers, L.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: J.Biol.Chem. / Year: 2024
Title: Structural analysis of the SAM domain of the Arabidopsis mitochondrial tRNA import receptor.
Authors: Olasz, B. / Smithers, L. / Evans, G.L. / Anandan, A. / Murcha, M.W. / Vrielink, A.
History
DepositionSep 27, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 1, 2024Provider: repository / Type: Initial release
Revision 1.1May 15, 2024Group: Database references / Category: citation / Item: _citation.journal_volume

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Chloroplastic import inner membrane translocase subunit HP30-1
B: Chloroplastic import inner membrane translocase subunit HP30-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,9524
Polymers20,4762
Non-polymers4772
Water1,45981
1
A: Chloroplastic import inner membrane translocase subunit HP30-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)10,4762
Polymers10,2381
Non-polymers2381
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Chloroplastic import inner membrane translocase subunit HP30-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)10,4762
Polymers10,2381
Non-polymers2381
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)46.579, 58.537, 61.949
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Space group name HallP2ac2ab
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x,y+1/2,-z+1/2
#4: -x+1/2,-y,z+1/2
DetailsThe assembly may be hexameric; however, the authors do not know the specific hexameric assembly.

-
Components

#1: Protein Chloroplastic import inner membrane translocase subunit HP30-1


Mass: 10237.844 Da / Num. of mol.: 2 / Fragment: SAM domain / Mutation: G241E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: HP30-1 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta 2 / References: UniProt: Q9SCK3
#2: Chemical ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES


Mass: 238.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H18N2O4S / Comment: pH buffer*YM
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 81 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2 Å3/Da / Density % sol: 38.48 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 8.2 / Details: 1.8-2.3 M ammonium sulphate, 0.1 M Tris / PH range: 8.0-8.7

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.953732 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Jun 6, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.953732 Å / Relative weight: 1
ReflectionResolution: 1.89→42.55 Å / Num. obs: 14037 / % possible obs: 99.6 % / Redundancy: 13.1 % / Biso Wilson estimate: 30.12 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.09 / Rpim(I) all: 0.03 / Net I/σ(I): 18.9
Reflection shellResolution: 1.89→1.96 Å / Redundancy: 13 % / Rmerge(I) obs: 1.5 / Mean I/σ(I) obs: 2.41 / Num. unique obs: 1355 / CC1/2: 0.0774 / Rpim(I) all: 0.42 / % possible all: 96.1

-
Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
PHENIX1.20.1_4487refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.89→42.55 Å / SU ML: 0.2322 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 24.538
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2368 756 5.41 %
Rwork0.1997 13213 -
obs0.2017 13969 99.2 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 41.78 Å2
Refinement stepCycle: LAST / Resolution: 1.89→42.55 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1011 0 30 81 1122
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0041077
X-RAY DIFFRACTIONf_angle_d0.72991455
X-RAY DIFFRACTIONf_chiral_restr0.0468168
X-RAY DIFFRACTIONf_plane_restr0.0125182
X-RAY DIFFRACTIONf_dihedral_angle_d7.326159
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.89-2.040.30391520.26562519X-RAY DIFFRACTION96.25
2.04-2.240.25511740.21562579X-RAY DIFFRACTION99.89
2.24-2.570.2221300.20822655X-RAY DIFFRACTION99.96
2.57-3.230.25811390.22332678X-RAY DIFFRACTION100
3.23-42.550.21951610.17492782X-RAY DIFFRACTION99.86
Refinement TLS params.

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

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
13.54860732654-0.4563666883021.537211640648.454246434414.351092988933.13023735349-0.351085122559-1.08486816185-0.8084121160930.7534364392740.4004478063410.4394063433931.18509573426-0.4625237238560.07622527939460.4479087241340.03344775771740.02382821801580.4063985630230.07025542934290.294550009368-8.705-5.51320.38
27.82831323261-5.219620502133.056757919173.74391123564-1.215807507683.95048475412-1.1192334211-1.24791974961-1.236385738020.4871891747050.4534174340340.3930363881311.268856613140.07853386965460.450868255860.6810745542320.1164863329030.2508265681420.3425278420950.1110648207170.392303942799-1.189-15.3220.745
32.76621943823-2.50789561344-0.4806295919695.38428347858-1.454106237292.48353672327-0.340712636381-1.103471423610.2315271281231.220155754840.470894371853-0.06557825820470.5757384825641.06160823648-0.0797711603390.46154746380.14470031586-0.09238521832680.433000278819-0.08093531863670.3624902354026.23-9.91417.184
49.84354602232-4.955383102990.2374632264826.419397778685.575431712638.62260400426-0.436627411273-0.1449469755130.06632005869910.3343748004880.2478025190450.182493515697-0.05230922766110.1066056449490.1634179657360.305376068127-0.004493374379580.02496418986060.1652216174520.00406063686570.199628227397-4.979-7.68612.6
53.2621028889-4.865022228023.187513596297.84335707837-3.697418287388.4395733948-0.01578556326530.6555673842860.0946803440156-0.137675383432-0.205556455386-0.467047565123-0.5313010264440.3715299840880.2559599608780.23083765376-0.02052550931620.05613059001890.194648551329-0.04503842508280.2715556419434.543-10.5636.287
62.90371925068-1.56919903631-3.532383000747.31214667045-1.175901127735.75935164530.2506391941390.102384037157-0.47692070291.59837835441-0.4128370925141.21171029986-0.221763961536-0.7270166051350.07746313069930.4837293603320.003211672012610.1728964818380.268311077906-0.06952274886610.448644688842.03-19.1639.194
71.70365939776-2.56968545402-1.664933409013.87300329032.50936258119.23285606254-0.005322556407030.444209290133-0.5790125487751.13024247029-0.108882788402-0.679314678481.78642801707-0.3230491630670.1133780895190.897713586492-0.2242868574610.03192055256240.9155210713610.3794509506951.425158896121.816-19.0357.571
87.425951324581.030238216744.596757348678.46171482001-0.1130597725753.0691857106-0.3099279225820.04417410222980.8034348017280.240089266494-0.34993576859-0.432146837203-1.106092077380.3563160656960.3805512150590.3398598968580.000668936605193-0.06270877186030.197837442557-0.04078438111480.31365927174-13.1156.6358.948
95.6572495309-0.3341616928252.45805507168.07121390118-2.979279697217.6307977615-0.194570587686-0.8243924540840.4852759857460.266469600679-0.05484370661530.710155735239-0.842397690683-0.8431589100540.06337317930030.2770127920760.055251898257-0.003034473916690.364908256173-0.09408693250930.242759649979-20.7692.0616.405
103.21293640032-0.2039403275014.627065873795.854896434322.828100073219.043279636560.0791907734419-0.0816813941452-0.04042633316470.397119750666-0.1611708855370.1844897155110.316633185293-0.5153043161380.05980414157910.207639991736-0.04016161918750.006554595459070.2148818388950.005128241309830.145062203957-14.731-6.2055.978
119.026350590822.86069350414-5.178365802837.25709080681-2.986037793313.475136761850.07316344630530.3587903772260.393419369861-0.0642854568321-0.212793646427-0.222288206085-0.5626997367310.1353600697030.1758589155830.316636378942-0.0295651763722-0.04177098908890.3168944352690.01372514809630.186214211028-13.942-2.113-4.35
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 191:196 )A191 - 196
2X-RAY DIFFRACTION2( CHAIN A AND RESID 197:206 )A197 - 206
3X-RAY DIFFRACTION3( CHAIN A AND RESID 207:217 )A207 - 217
4X-RAY DIFFRACTION4( CHAIN A AND RESID 218:227 )A218 - 227
5X-RAY DIFFRACTION5( CHAIN A AND RESID 228:239 )A228 - 239
6X-RAY DIFFRACTION6( CHAIN A AND RESID 240:251 )A240 - 251
7X-RAY DIFFRACTION7( CHAIN A AND RESID 252:253 )A252 - 253
8X-RAY DIFFRACTION8( CHAIN B AND RESID 192:205 )B192 - 205
9X-RAY DIFFRACTION9( CHAIN B AND RESID 206:217 )B206 - 217
10X-RAY DIFFRACTION10( CHAIN B AND RESID 218:239 )B218 - 239
11X-RAY DIFFRACTION11( CHAIN B AND RESID 240:253 )B240 - 253

+
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://pdbjlvh1.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