[English] 日本語
Yorodumi
- PDB-6byd: Crystal structure of the second StART domain of yeast Lam4 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6byd
TitleCrystal structure of the second StART domain of yeast Lam4
ComponentsMembrane-anchored lipid-binding protein LAM4
KeywordsLIPID TRANSPORT / Sterol Transport
Function / homology
Function and homology information


intracellular sterol transport / endoplasmic reticulum-plasma membrane contact site / sterol transfer activity / sterol binding / cortical endoplasmic reticulum / endoplasmic reticulum membrane / mitochondrion / plasma membrane
Similarity search - Function
VASt domain / VAD1 Analog of StAR-related lipid transfer domain / VASt domain profile. / domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins / GRAM domain / GRAM domain / PH-like domain superfamily
Similarity search - Domain/homology
Membrane-anchored lipid-binding protein LAM4
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.195 Å
AuthorsJentsch, J.A. / Kiburu, I.N. / Wu, J. / Pandey, K. / Boudker, O. / Menon, A.K.
Funding support Germany, Qatar, 2items
OrganizationGrant numberCountry
German Research Foundation (DFG)Graduiertenkolleg 2098, Project 11 Germany
Qatar National Research FundNPRP 7-082-1-014Qatar
CitationJournal: J. Biol. Chem. / Year: 2018
Title: Structural basis of sterol binding and transport by a yeast StARkin domain.
Authors: Jentsch, J.A. / Kiburu, I. / Pandey, K. / Timme, M. / Ramlall, T. / Levkau, B. / Wu, J. / Eliezer, D. / Boudker, O. / Menon, A.K.
History
DepositionDec 20, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 31, 2018Provider: repository / Type: Initial release
Revision 1.1Feb 14, 2018Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2Mar 7, 2018Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.name
Revision 1.3Apr 25, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.4Jan 8, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Membrane-anchored lipid-binding protein LAM4


Theoretical massNumber of molelcules
Total (without water)23,0401
Polymers23,0401
Non-polymers00
Water86548
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area9980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)45.601, 67.923, 132.042
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number24
Space group name H-MI212121

-
Components

#1: Protein Membrane-anchored lipid-binding protein LAM4 / Lipid transfer at contact site protein 3 / Lipid transfer protein anchored at membrane contact sites 1


Mass: 23040.311 Da / Num. of mol.: 1 / Fragment: LAM4 (YHR080C)-StARkin domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: LAM4, LTC3, YHR080C / Production host: Escherichia coli (E. coli) / References: UniProt: P38800
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 48 / 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: 2.3 Å3/Da / Density % sol: 46.49 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion
Details: 0.5M Lithium Chloride 30% PEG 6000 0.1M HEPES, pH 7.5

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 0.97494 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 28, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97494 Å / Relative weight: 1
ReflectionResolution: 2.19→50 Å / Num. obs: 11009 / % possible obs: 100 % / Redundancy: 14 % / Biso Wilson estimate: 30.88 Å2 / Rmerge(I) obs: 0.132 / Rpim(I) all: 0.037 / Rrim(I) all: 0.137 / Χ2: 0.981 / Net I/σ(I): 7.3 / Num. measured all: 153681
Reflection shell

Diffraction-ID: 1 / % possible all: 100

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2
2.19-2.2712.80.66410830.9680.1890.6910.614
2.27-2.36140.51110860.9860.1410.5310.492
2.36-2.4714.40.41710590.9790.1140.4320.556
2.47-2.614.50.30611030.9910.0840.3180.639
2.6-2.7614.40.24410730.9910.0670.2540.855
2.76-2.9714.40.18310900.9920.050.1891.092
2.97-3.2714.20.13411100.9960.0370.1391.338
3.27-3.7414.10.1210980.9960.0330.1251.381
3.74-4.7213.60.0911110.9950.0250.0941.423
4.72-5013.30.07811960.9970.0220.0811.376

-
Processing

Software
NameVersionClassification
PHENIX1.11.1_2575refinement
HKL-2000data reduction
HKL-2000data scaling
PDB_EXTRACT3.24data extraction
HKL2Mapphasing
RefinementResolution: 2.195→43.103 Å / SU ML: 0.19 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 29.62 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.248 544 5.02 %
Rwork0.1857 10293 -
obs0.189 10837 99.61 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 131.23 Å2 / Biso mean: 45.1961 Å2 / Biso min: 18.41 Å2
Refinement stepCycle: final / Resolution: 2.195→43.103 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1553 0 0 48 1601
Biso mean---42.04 -
Num. residues----197
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0081582
X-RAY DIFFRACTIONf_angle_d0.9012141
X-RAY DIFFRACTIONf_chiral_restr0.056248
X-RAY DIFFRACTIONf_plane_restr0.006273
X-RAY DIFFRACTIONf_dihedral_angle_d3.585979
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 4

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.1946-2.41550.28021260.21552506263299
2.4155-2.76490.28911360.20925302666100
2.7649-3.48330.27461340.200525742708100
3.4833-43.11130.21761480.16526832831100
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)
12.2687-0.25830.13191.7386-1.08531.071-0.19060.19190.1046-0.2350.14890.256-0.2675-0.88340.06840.3740.0587-0.04590.788-0.01980.360814.295635.2951.5139
21.8194-0.2522-0.46032.27460.63773.55210.12750.012-0.233-0.2193-0.19570.05220.1351-0.60860.0130.2111-0.0015-0.020.28150.00030.254422.116931.146451.4533
34.6853-1.3567-0.79472.9526-0.18752.30170.10110.0503-0.0747-0.1229-0.19720.21770.07360.31750.09570.1884-0.0005-0.01310.3650.00060.197337.669634.980556.0051
43.9064-0.4139-0.34092.01660.07013.43930.12110.1730.0265-0.299-0.1770.02780.04340.40910.01670.30330.03640.01820.2219-0.00490.201237.306335.520446.3725
52.3783-2.43471.28363.7245-0.21352.5551-0.9033-1.07380.34880.28970.6908-0.0044-0.3554-0.10960.08370.28260.0566-0.00170.2764-0.03690.200232.214136.4544.1685
66.601-0.5543-0.94142.9015-0.22153.09280.40290.09760.8459-0.5569-0.1449-0.13590.0387-0.9833-0.04180.22880.1164-0.02150.35150.02690.305921.864335.892545.0863
73.9834-0.9155-0.39261.20891.07263.58950.0016-0.1279-0.0615-0.0715-0.12260.09190.412-0.42960.00790.2983-0.0043-0.03520.21620.01010.262226.316529.420546.2041
80.82441.2734-0.36322.0262-0.86095.0175-0.3710.1482-0.5395-0.262-0.2152-0.38831.05780.49260.17440.47610.14930.05930.2977-0.03670.347934.381524.175433.4529
91.6457-0.3963-1.26661.81840.63414.04980.0796-0.3211-0.1417-0.1965-0.0612-0.08490.56250.04080.00710.35280.0591-0.01430.19240.05450.2929.490426.673154.8422
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 4 through 23 )A4 - 23
2X-RAY DIFFRACTION2chain 'A' and (resid 24 through 50 )A24 - 50
3X-RAY DIFFRACTION3chain 'A' and (resid 51 through 70 )A51 - 70
4X-RAY DIFFRACTION4chain 'A' and (resid 71 through 98 )A71 - 98
5X-RAY DIFFRACTION5chain 'A' and (resid 99 through 111 )A99 - 111
6X-RAY DIFFRACTION6chain 'A' and (resid 112 through 124 )A112 - 124
7X-RAY DIFFRACTION7chain 'A' and (resid 125 through 153 )A125 - 153
8X-RAY DIFFRACTION8chain 'A' and (resid 154 through 166 )A154 - 166
9X-RAY DIFFRACTION9chain 'A' and (resid 167 through 200 )A167 - 200

+
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