[English] 日本語
Yorodumi
- PDB-3skq: Mdm38 is a 14-3-3-like receptor and associates with the protein s... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3skq
TitleMdm38 is a 14-3-3-like receptor and associates with the protein synthesis machinery at the inner mitochondrial membrane
ComponentsMitochondrial distribution and morphology protein 38
KeywordsMETAL TRANSPORT / 14-3-3-like membrane protein / mitochondrial ribosome / respiratory chain biogenesis / Letm1 homolog / 14-3-3 like fold / Ribosome binding receptor / Ribosomes / Mitochondrial inner membrane
Function / homology
Function and homology information


: / protein insertion into mitochondrial inner membrane from matrix / mitochondrial ribosome binding / intracellular potassium ion homeostasis / positive regulation of mitochondrial translation / proton transmembrane transport / potassium ion transport / mitochondrial inner membrane / membrane => GO:0016020 / mitochondrion
Similarity search - Function
: / LETM1-like, ribosome-binding domain / LETM1-like, RBD / Letm1 ribosome-binding (RBD) domain profile.
Similarity search - Domain/homology
IODIDE ION / : / Mitochondrial distribution and morphology protein 38
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsLupo, D. / Tews, I. / Sinning, I.
CitationJournal: Traffic / Year: 2011
Title: Mdm38 is a 14-3-3-Like Receptor and Associates with the Protein Synthesis Machinery at the Inner Mitochondrial Membrane.
Authors: Lupo, D. / Vollmer, C. / Deckers, M. / Mick, D.U. / Tews, I. / Sinning, I. / Rehling, P.
History
DepositionJun 23, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 27, 2011Provider: repository / Type: Initial release
Revision 1.1Sep 28, 2011Group: Database references
Revision 1.2Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_special_symmetry / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Mitochondrial distribution and morphology protein 38
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,92710
Polymers28,8731
Non-polymers1,0549
Water2,684149
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)124.527, 52.033, 47.232
Angle α, β, γ (deg.)90.00, 108.65, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-3-

IOD

-
Components

#1: Protein Mitochondrial distribution and morphology protein 38


Mass: 28873.141 Da / Num. of mol.: 1 / Fragment: C-terminal fragment, UNP residues 160-408
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: MDM38, YOL027C / Plasmid: pGEX4t3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Codon Plus R (DE3) -Ril / References: UniProt: Q08179
#2: Chemical
ChemComp-IOD / IODIDE ION / Iodide


Mass: 126.904 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: I
#3: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 149 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.51 Å3/Da / Density % sol: 51.01 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7
Details: 0.25M KI and 21% PEG3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.9334 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Nov 5, 2009 / Details: mirrors
RadiationMonochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9334 Å / Relative weight: 1
ReflectionResolution: 2.1→30 Å / Num. all: 44933 / Num. obs: 16561 / % possible obs: 97.8 % / Observed criterion σ(F): 3 / Observed criterion σ(I): 3 / Redundancy: 3 % / Biso Wilson estimate: 35.4 Å2 / Rmerge(I) obs: 0.144 / Rsym value: 0.051 / Net I/σ(I): 15.8
Reflection shellResolution: 2.1→2.2 Å / Rmerge(I) obs: 0.762 / Mean I/σ(I) obs: 3.11 / Num. unique all: 2141 / Rsym value: 0.405 / % possible all: 97.6

-
Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHASERphasing
PHENIX(phenix.refine: 1.7_650)refinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→30 Å / SU ML: 0.31 / σ(F): 1.35 / Phase error: 24.55 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2266 831 5.02 %Random
Rwork0.1947 ---
all0.1964 44933 --
obs0.1964 16560 97.97 %-
Solvent computationShrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 35.288 Å2 / ksol: 0.352 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--2.2477 Å20 Å2-4.9634 Å2
2--9.9026 Å20 Å2
3----7.6549 Å2
Refinement stepCycle: LAST / Resolution: 2.1→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1849 0 9 149 2007
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0081881
X-RAY DIFFRACTIONf_angle_d0.9672526
X-RAY DIFFRACTIONf_dihedral_angle_d13.263731
X-RAY DIFFRACTIONf_chiral_restr0.071279
X-RAY DIFFRACTIONf_plane_restr0.004321
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1-2.23160.33091330.26712599X-RAY DIFFRACTION98
2.2316-2.40390.28971350.22952628X-RAY DIFFRACTION98
2.4039-2.64580.27841400.23012613X-RAY DIFFRACTION99
2.6458-3.02850.26211230.19612638X-RAY DIFFRACTION98
3.0285-3.81520.2111460.17872629X-RAY DIFFRACTION99
3.8152-42.86860.1791540.17132622X-RAY DIFFRACTION96
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)
10.639-0.5080.47311.4613-0.92681.7898-0.0931-0.22050.79490.2603-0.2923-0.3176-0.32130.4594-0.26550.2833-0.0077-0.05410.1668-0.10210.240247.200419.685120.1424
20.39-0.54180.3370.9451-0.17690.96090.1220.64370.0754-0-0.0947-0.24330.21970.6376-0.02910.23660.12520.03640.38130.00220.213653.33844.1719-0.1542
31.48020.07840.6791.4046-0.17831.36720.0147-0.17060.02430.1384-0.1554-0.10450.00880.08240.03320.16050.03130.00170.1486-0.01990.17945.746910.185311.1934
41.02850.04810.01961.3567-0.16121.24560.2133-0.3213-0.33870.21930.00230.33630.1252-0.3789-0.05360.2073-0.02970.03150.24320.01060.238932.26634.120717.9688
50.7021-0.00240.18450.4792-0.03080.2797-0.0879-0.15440.08640.32190.00320.5384-0.3091-0.35190.05030.21720.09150.0780.4099-0.0580.330624.109817.326515.3595
60.6101-0.15970.08020.4253-0.25740.7527-0.0701-0.06590.2121-0.14550.13750.0383-0.3076-0.23940.01090.22250.06430.00020.1912-0.01620.292329.568718.45219.5037
71.108-0.18650.43920.2649-0.4040.78090.04560.27270.0989-0.01470.09740.09850.0175-0.03210.01720.15920.00780.0130.13890.0070.181539.527511.33588.9213
81.25460.42530.11450.6581-0.6430.96720.07260.14570.26830.28090.2784-0.0075-0.47620.18980.11670.485-0.10540.09310.45120.08230.422649.810124.28317.5491
91.1858-0.09460.95970.9655-0.51221.38-0.05670.33910.1916-0.2143-0.21080.091-0.23510.21640.0730.1770.0485-0.02240.2298-0.01510.200435.5520.911-8.3317
100.3590.63940.00781.114-0.0931.4207-0.0191-0.18310.2992-0.1053-0.0469-0.1664-0.05530.15850.0520.19030.00450.02510.16320.00210.186245.364515.35933.6501
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 182:200)
2X-RAY DIFFRACTION2chain 'A' and (resseq 201:227)
3X-RAY DIFFRACTION3chain 'A' and (resseq 228:276)
4X-RAY DIFFRACTION4chain 'A' and (resseq 277:301)
5X-RAY DIFFRACTION5chain 'A' and (resseq 302:318)
6X-RAY DIFFRACTION6chain 'A' and (resseq 319:342)
7X-RAY DIFFRACTION7chain 'A' and (resseq 343:358)
8X-RAY DIFFRACTION8chain 'A' and (resseq 359:367)
9X-RAY DIFFRACTION9chain 'A' and (resseq 368:382)
10X-RAY DIFFRACTION10chain 'A' and (resseq 383:408)

+
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