[English] 日本語
Yorodumi
- PDB-3pvl: Structure of myosin VIIa MyTH4-FERM-SH3 in complex with the CEN1 ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3pvl
TitleStructure of myosin VIIa MyTH4-FERM-SH3 in complex with the CEN1 of Sans
Components
  • Myosin VIIa isoform 1
  • Usher syndrome type-1G protein
KeywordsMOTOR PROTEIN/PROTEIN TRANSPORT / protein complex / Novel folding / protein cargo binding / cargo proteins / MOTOR PROTEIN-PROTEIN TRANSPORT complex
Function / homology
Function and homology information


: / photoreceptor cell cilium / pigment granule localization / upper tip-link density / pigment granule transport / stereocilium base / The canonical retinoid cycle in rods (twilight vision) / microfilament motor activity => GO:0000146 / myosin VII complex / phagolysosome assembly ...: / photoreceptor cell cilium / pigment granule localization / upper tip-link density / pigment granule transport / stereocilium base / The canonical retinoid cycle in rods (twilight vision) / microfilament motor activity => GO:0000146 / myosin VII complex / phagolysosome assembly / inner ear receptor cell differentiation / protein localization => GO:0008104 / regulation of clathrin-dependent endocytosis / equilibrioception / mechanoreceptor differentiation / sensory perception of light stimulus / photoreceptor connecting cilium / actin filament-based movement / inner ear receptor cell stereocilium organization / sensory organ development / : / inner ear auditory receptor cell differentiation / sensory perception / stereocilium / cell projection organization / vesicle transport along actin filament / photoreceptor cell maintenance / auditory receptor cell stereocilium organization / Sensory processing of sound by outer hair cells of the cochlea / Sensory processing of sound by inner hair cells of the cochlea / myosin complex / microfilament motor activity / ciliary base / inner ear morphogenesis / spectrin binding / lysosome organization / cochlea development / inner ear development / microvillus / cytoskeletal motor activity / photoreceptor outer segment / Cajal body / phagocytosis / photoreceptor inner segment / visual perception / ciliary basal body / actin filament organization / ADP binding / sensory perception of sound / intracellular protein transport / protein localization / actin filament binding / melanosome / actin cytoskeleton / actin binding / cell cortex / vesicle / calmodulin binding / nuclear speck / apical plasma membrane / lysosomal membrane / protein domain specific binding / centrosome / synapse / protein-containing complex binding / ATP binding / identical protein binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
USH1G, SAM domain / MyTH4 domain / Class VII myosin, motor domain / Myosin VII, FERM domain C-lobe, repeat 1 / Myosin VII, FERM domain C-lobe, repeat 2 / MyTH4 domain / MyTH4 domain superfamily / MyTH4 domain / MyTH4 domain profile. / Domain in Myosin and Kinesin Tails ...USH1G, SAM domain / MyTH4 domain / Class VII myosin, motor domain / Myosin VII, FERM domain C-lobe, repeat 1 / Myosin VII, FERM domain C-lobe, repeat 2 / MyTH4 domain / MyTH4 domain superfamily / MyTH4 domain / MyTH4 domain profile. / Domain in Myosin and Kinesin Tails / Acyl-CoA Binding Protein - #10 / Acyl-CoA Binding Protein / IQ calmodulin-binding motif / Myosin S1 fragment, N-terminal / SAM domain (Sterile alpha motif) / FERM central domain / FERM/acyl-CoA-binding protein superfamily / 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 / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / FERM central domain / SH3 Domains / PH-domain like / FERM superfamily, second domain / FERM domain / FERM domain profile. / Band 4.1 domain / Band 4.1 homologues / Kinesin motor domain superfamily / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / SH3 type barrels. / Src homology 3 domains / Ubiquitin-like (UB roll) / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Alpha Horseshoe / PH-like domain superfamily / Ubiquitin-like domain superfamily / Roll / Roll / Up-down Bundle / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHOSPHATE ION / Unconventional myosin-VIIa / pre-mRNA splicing regulator USH1G / Unconventional myosin-VIIa
Similarity search - Component
Biological speciesMus musculus (house mouse)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.8 Å
AuthorsWu, L. / Pan, L.F. / Wei, Z.Y. / Zhang, M.J.
CitationJournal: Science / Year: 2011
Title: Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo.
Authors: Wu, L. / Pan, L. / Wei, Z. / Zhang, M.
History
DepositionDec 7, 2010Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Mar 2, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Mar 20, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _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: Myosin VIIa isoform 1
B: Usher syndrome type-1G protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,58813
Polymers84,5692
Non-polymers1,01911
Water68538
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2280 Å2
ΔGint-10 kcal/mol
Surface area28970 Å2
MethodPISA
Unit cell
Length a, b, c (Å)98.864, 98.864, 242.278
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121

-
Components

#1: Protein Myosin VIIa isoform 1


Mass: 74353.219 Da / Num. of mol.: 1 / Fragment: MyTH4-FERM-SH3 region
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Myo7a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q5MJ57, UniProt: P97479*PLUS
#2: Protein Usher syndrome type-1G protein / Scaffold protein containing ankyrin repeats and SAM domain


Mass: 10215.873 Da / Num. of mol.: 1 / Fragment: Central region of Sans, the CEN1 motif
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: USH1G, SANS / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q495M9
#3: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: PO4
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 38 / 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: 4.04 Å3/Da / Density % sol: 69.57 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 0.02M MgCl2, 0.1M HEPES, pH 7.5, 22% (w/v) polyacrylic acid sodium salt 5100, VAPOR DIFFUSION, HANGING DROP, temperature 289K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 1.5418 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 27, 2009
RadiationMonochromator: MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. all: 34633 / Num. obs: 32761 / % possible obs: 99.57 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 9.1 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 31
Reflection shellResolution: 2.801→2.874 Å / Redundancy: 9.3 % / Rmerge(I) obs: 0.06 / Mean I/σ(I) obs: 31 / Num. unique all: 34633 / % possible all: 99.69

-
Processing

Software
NameVersionClassification
HKL-2000data collection
SHARPphasing
REFMAC5.5.0072refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: SAD / Resolution: 2.8→50 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.915 / SU B: 11.315 / SU ML: 0.222 / Cross valid method: THROUGHOUT / σ(F): 3.7 / σ(I): 3.7 / ESU R Free: 0.289 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25903 1740 5 %RANDOM
Rwork0.22764 ---
all0.22922 34633 --
obs0.22922 32761 99.57 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 67.928 Å2
Baniso -1Baniso -2Baniso -3
1-0.17 Å20.08 Å20 Å2
2--0.17 Å20 Å2
3----0.25 Å2
Refinement stepCycle: LAST / Resolution: 2.8→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4888 0 64 38 4990
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0225066
X-RAY DIFFRACTIONr_angle_refined_deg0.981.9726852
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.925610
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.23923.465228
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.83615855
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.9261535
X-RAY DIFFRACTIONr_chiral_restr0.0690.2748
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0213799
X-RAY DIFFRACTIONr_mcbond_it1.40223062
X-RAY DIFFRACTIONr_mcangle_it2.64534950
X-RAY DIFFRACTIONr_scbond_it3.3842004
X-RAY DIFFRACTIONr_scangle_it5.58561901
LS refinement shellResolution: 2.801→2.874 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.39 134 -
Rwork0.352 2418 -
obs--99.69 %

+
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