[English] 日本語
Yorodumi
- PDB-6kz1: Complex structure of Whirlin and Myosin XVa -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6kz1
TitleComplex structure of Whirlin and Myosin XVa
Components
  • Myosin XVa
  • Whirlin
KeywordsMOTOR PROTEIN / Whirlin / Myosin XVa / complex structure
Function / homology
Function and homology information


paranodal junction maintenance / microfilament motor activity => GO:0000146 / periciliary membrane compartment / USH2 complex / stereocilia ankle link / actin-based cell projection / inner ear receptor cell differentiation / stereocilia ankle link complex / sensory perception of light stimulus / cerebellar Purkinje cell layer formation ...paranodal junction maintenance / microfilament motor activity => GO:0000146 / periciliary membrane compartment / USH2 complex / stereocilia ankle link / actin-based cell projection / inner ear receptor cell differentiation / stereocilia ankle link complex / sensory perception of light stimulus / cerebellar Purkinje cell layer formation / photoreceptor connecting cilium / stereocilium tip / inner ear receptor cell stereocilium organization / detection of mechanical stimulus involved in sensory perception of sound / stereocilium / vesicle transport along actin filament / retina homeostasis / auditory receptor cell stereocilium organization / myosin complex / Sensory processing of sound by outer hair cells of the cochlea / Sensory processing of sound by inner hair cells of the cochlea / microfilament motor activity / photoreceptor inner segment / ciliary basal body / establishment of localization in cell / actin filament / actin filament organization / sensory perception of sound / establishment of protein localization / cilium / actin filament binding / actin cytoskeleton / growth cone / vesicle / calmodulin binding / synapse / positive regulation of gene expression / extracellular exosome / ATP binding / identical protein binding / plasma membrane / cytoplasm
Similarity search - Function
Unconventional myosin-XV / Whirlin / : / Class XV myosin, motor domain / Myosin-XV, FERM domain C-lobe / MyTH4 domain / MyTH4 domain superfamily / MyTH4 domain / MyTH4 domain profile. / Domain in Myosin and Kinesin Tails ...Unconventional myosin-XV / Whirlin / : / Class XV myosin, motor domain / Myosin-XV, FERM domain C-lobe / MyTH4 domain / MyTH4 domain superfamily / MyTH4 domain / MyTH4 domain profile. / Domain in Myosin and Kinesin Tails / IQ calmodulin-binding motif / Variant SH3 domain / Short calmodulin-binding motif containing conserved Ile and Gln residues. / Myosin head, motor domain / Myosin head (motor domain) / Myosin motor domain profile. / Myosin. Large ATPases. / IQ motif profile. / IQ motif, EF-hand binding site / FERM central domain / FERM superfamily, second domain / FERM domain / FERM domain profile. / Band 4.1 domain / Band 4.1 homologues / Kinesin motor domain superfamily / PDZ domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / PH-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Whirlin / Unconventional myosin-XV
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.694 Å
AuthorsLin, L. / Wang, M. / Shi, Y. / Zhu, J. / Zhang, R.
CitationJournal: Cell Rep / Year: 2021
Title: Phase separation-mediated condensation of Whirlin-Myo15-Eps8 stereocilia tip complex.
Authors: Lin, L. / Shi, Y. / Wang, M. / Wang, C. / Lu, Q. / Zhu, J. / Zhang, R.
History
DepositionSep 22, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 23, 2020Provider: repository / Type: Initial release
Revision 1.1Apr 7, 2021Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 22, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Whirlin
B: Myosin XVa


Theoretical massNumber of molelcules
Total (without water)14,0422
Polymers14,0422
Non-polymers00
Water95553
1
A: Whirlin

B: Myosin XVa


Theoretical massNumber of molelcules
Total (without water)14,0422
Polymers14,0422
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-y+1,x-y+1,z+1/31
Buried area1160 Å2
ΔGint-11 kcal/mol
Surface area6130 Å2
MethodPISA
Unit cell
Length a, b, c (Å)51.974, 51.974, 70.445
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number152
Space group name H-MP3121
Components on special symmetry positions
IDModelComponents
11A-1023-

HOH

-
Components

#1: Protein Whirlin / Autosomal recessive deafness type 31 protein


Mass: 12430.313 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: WHRN, DFNB31, KIAA1526 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9P202
#2: Protein/peptide Myosin XVa


Mass: 1611.920 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q9UKN7*PLUS
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 53 / 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: 1.96 Å3/Da / Density % sol: 37.12 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop
Details: Potassium phosphate dibasic, HEPES pH7.5, Sodium phosphate monobasi

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 12, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.69→45.011 Å / Num. obs: 23647 / % possible obs: 99.8 % / Redundancy: 10.261 % / CC1/2: 0.999 / Rmerge(I) obs: 0.055 / Rrim(I) all: 0.057 / Χ2: 1.13 / Net I/σ(I): 22.54 / Num. measured all: 242635
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
1.69-1.89.8130.6853.1237386385938100.9280.72298.7
1.8-1.9210.3190.396.2236695355735560.9820.411100
1.92-2.0710.860.20112.2936632337333730.9950.211100
2.07-2.2710.6180.12119.8632692307930790.9970.127100
2.27-2.549.6650.08425.5826819277527750.9980.089100
2.54-2.939.9660.06234.0624765248524850.9990.066100
2.93-3.5810.660.04748.6621927205720570.9990.049100
3.58-5.0510.1040.03855.1116368162016200.9990.04100
5.05-45.01110.4830.03557.7193518928920.9990.037100

-
Processing

Software
NameVersionClassification
XDSdata scaling
PHENIX1.8.4_1496refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1UFX
Resolution: 1.694→45.011 Å / SU ML: 0.16 / Cross valid method: THROUGHOUT / σ(F): 1.39 / Phase error: 21.6
RfactorNum. reflection% reflection
Rfree0.2008 637 5.03 %
Rwork0.1787 --
obs0.1798 12670 99.72 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 86.41 Å2 / Biso mean: 34.83 Å2 / Biso min: 17.83 Å2
Refinement stepCycle: final / Resolution: 1.694→45.011 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms811 0 0 53 864
Biso mean---42.96 -
Num. residues----109
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.012819
X-RAY DIFFRACTIONf_angle_d1.4241108
X-RAY DIFFRACTIONf_chiral_restr0.06137
X-RAY DIFFRACTIONf_plane_restr0.007141
X-RAY DIFFRACTIONf_dihedral_angle_d13.155301
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.694-1.82470.2411260.2211233399
1.8247-2.00830.23131280.18722371100
2.0083-2.29890.18731290.17272379100
2.2989-2.89640.24121230.20852423100
2.8964-45.0110.18251310.16452527100
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)
10.16490.34060.25240.70610.66490.61750.0002-0.4190.04210.1469-0.09070.15140.0667-0.2076-0.08820.2229-0.0805-0.0310.31020.01430.228-11.032717.75465.8321
21.25020.66320.73180.65410.26880.4729-0.83070.19410.9039-0.820.20230.5284-0.6746-0.1388-0.01110.2807-0.0834-0.08680.25880.00920.2452-10.216625.4206-6.9816
30.03810.02810.0360.03940.01640.01520.1848-0.4660.5580.38910.0653-0.08140.1040.4163-0.00030.2459-0.0266-0.00860.3238-0.05120.27315.694327.21161.9601
40.0778-0.0498-0.08990.08030.05230.1125-0.26960.39980.3992-0.36090.29420.1342-0.21660.3255-0.00090.2828-0.0514-0.04580.18240.02670.2738-6.958931.589-0.2822
50.34840.5138-0.03170.5660.12170.26290.0951-0.0369-0.0638-0.0408-0.15060.3093-0.0143-0.0957-0.00020.2423-0.0064-0.05690.2354-0.03240.2833-11.667925.40970.3936
60.0813-0.0683-0.06710.11530.11360.1030.06240.2648-0.88020.036-0.0135-0.37440.27730.4995-0.00280.23480.0002-0.06310.31160.00630.33992.790717.5046-0.0431
70.0095-0.00610.01180.12420.13530.0624-0.63840.8327-0.3513-0.66220.5429-0.0475-0.11770.31080.00070.3012-0.0780.04620.3479-0.06640.2528-1.383719.92-8.8304
80.8049-0.2626-0.40580.2550.21690.4541-0.1923-0.254-0.67610.47790.0185-0.02150.55840.1024-0.0010.3162-0.03260.0370.2195-0.02850.4497-12.299410.6831-9.6896
90.1186-0.013-0.02790.0473-0.06410.07050.0088-0.0696-0.29830.20970.0369-0.20260.0677-0.07880.00110.2583-0.0483-0.0290.24040.00840.2399-9.031217.64791.6248
100.0240.0730.03530.07450.01770.05350.3902-0.0671-0.38980.4837-0.1029-0.19240.029-0.3226-0.00240.3667-0.037-0.01420.4003-0.04090.25720.334827.885911.2051
110.04540.1098-0.01240.0254-0.01050.1221-0.1268-0.51770.004-0.3547-0.169-0.13870.14910.21480.00110.2741-0.0526-0.00940.34960.04390.30123.912234.3247-11.9894
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 811 through 820 )A811 - 820
2X-RAY DIFFRACTION2chain 'A' and (resid 821 through 831 )A821 - 831
3X-RAY DIFFRACTION3chain 'A' and (resid 832 through 841 )A832 - 841
4X-RAY DIFFRACTION4chain 'A' and (resid 842 through 846 )A842 - 846
5X-RAY DIFFRACTION5chain 'A' and (resid 847 through 867 )A847 - 867
6X-RAY DIFFRACTION6chain 'A' and (resid 868 through 876 )A868 - 876
7X-RAY DIFFRACTION7chain 'A' and (resid 877 through 889 )A877 - 889
8X-RAY DIFFRACTION8chain 'A' and (resid 890 through 894 )A890 - 894
9X-RAY DIFFRACTION9chain 'A' and (resid 895 through 901 )A895 - 901
10X-RAY DIFFRACTION10chain 'A' and (resid 902 through 907 )A902 - 907
11X-RAY DIFFRACTION11chain 'B' and (resid 3500 through 3511 )B0

+
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