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- PDB-5yk5: structure of the human Lamtor4-Lamtor5 complex -

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Basic information

Entry
Database: PDB / ID: 5yk5
Titlestructure of the human Lamtor4-Lamtor5 complex
Components
  • (Ragulator complex protein LAMTOR4) x 2
  • (Ragulator complex protein LAMTOR5) x 2
KeywordsSIGNALING PROTEIN / cellular signal transduction pathway
Function / homology
Function and homology information


FNIP-folliculin RagC/D GAP / Ragulator complex / protein localization to lysosome / MTOR signalling / Energy dependent regulation of mTOR by LKB1-AMPK / Amino acids regulate mTORC1 / TORC1 signaling / Macroautophagy / regulation of cell size / mTORC1-mediated signalling ...FNIP-folliculin RagC/D GAP / Ragulator complex / protein localization to lysosome / MTOR signalling / Energy dependent regulation of mTOR by LKB1-AMPK / Amino acids regulate mTORC1 / TORC1 signaling / Macroautophagy / regulation of cell size / mTORC1-mediated signalling / positive regulation of TOR signaling / positive regulation of TORC1 signaling / viral genome replication / Regulation of PTEN gene transcription / positive regulation of interleukin-8 production / TP53 Regulates Metabolic Genes / cellular response to amino acid stimulus / positive regulation of protein localization to nucleus / response to virus / late endosome membrane / positive regulation of canonical NF-kappaB signal transduction / lysosome / intracellular membrane-bounded organelle / lysosomal membrane / positive regulation of gene expression / negative regulation of apoptotic process / protein-containing complex / cytosol
Similarity search - Function
Ragulator complex protein LAMTOR4 / Ragulator complex protein LAMTOR5 / Ragulator complex protein LAMTOR5 / Dynein light chain 2a, cytoplasmic / Beta-Lactamase / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Ragulator complex protein LAMTOR5 / Ragulator complex protein LAMTOR4
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.03 Å
AuthorsWu, G. / Mu, Z.
CitationJournal: Cell Discov / Year: 2017
Title: Structural insight into the Ragulator complex which anchors mTORC1 to the lysosomal membrane
Authors: Mu, Z. / Wang, L. / Deng, W. / Wang, J. / Wu, G.
History
DepositionOct 12, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 12, 2018Provider: repository / Type: Initial release
Revision 1.1Jan 23, 2019Group: Data collection / 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 1.2Mar 27, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / refine_hist / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine_hist.d_res_low / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ragulator complex protein LAMTOR4
B: Ragulator complex protein LAMTOR5
C: Ragulator complex protein LAMTOR4
D: Ragulator complex protein LAMTOR5


Theoretical massNumber of molelcules
Total (without water)36,7274
Polymers36,7274
Non-polymers00
Water1,22568
1
A: Ragulator complex protein LAMTOR4
B: Ragulator complex protein LAMTOR5


Theoretical massNumber of molelcules
Total (without water)18,5422
Polymers18,5422
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2060 Å2
ΔGint-12 kcal/mol
Surface area9410 Å2
MethodPISA
2
C: Ragulator complex protein LAMTOR4
D: Ragulator complex protein LAMTOR5


Theoretical massNumber of molelcules
Total (without water)18,1852
Polymers18,1852
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2040 Å2
ΔGint-11 kcal/mol
Surface area9080 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.672, 76.672, 52.939
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number145
Space group name H-MP32
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
12B
22D

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11LEULEUARGARGAA9 - 921 - 84
21LEULEUALAALACC9 - 921 - 84
12THRTHRLYSLYSBB4 - 883 - 87
22THRTHRLYSLYSDD4 - 881 - 85

NCS ensembles :
ID
1
2

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Components

#1: Protein Ragulator complex protein LAMTOR4 / Late endosomal/lysosomal adaptor and MAPK and MTOR activator 4


Mass: 9195.485 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: LAMTOR4, C7orf59 / Production host: Escherichia coli (E. coli) / References: UniProt: Q0VGL1
#2: Protein Ragulator complex protein LAMTOR5 / Hepatitis B virus X-interacting protein / HBX-interacting protein / Late endosomal/lysosomal ...Hepatitis B virus X-interacting protein / HBX-interacting protein / Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5


Mass: 9346.591 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: LAMTOR5, HBXIP, XIP / Production host: Escherichia coli (E. coli) / References: UniProt: O43504
#3: Protein Ragulator complex protein LAMTOR4 / Late endosomal/lysosomal adaptor and MAPK and MTOR activator 4


Mass: 9051.334 Da / Num. of mol.: 1 / Mutation: E10A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: LAMTOR4, C7orf59 / Production host: Escherichia coli (E. coli) / References: UniProt: Q0VGL1
#4: Protein Ragulator complex protein LAMTOR5 / Hepatitis B virus X-interacting protein / HBX-interacting protein / Late endosomal/lysosomal ...Hepatitis B virus X-interacting protein / HBX-interacting protein / Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5


Mass: 9133.357 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: LAMTOR5, HBXIP, XIP / Production host: Escherichia coli (E. coli) / References: UniProt: O43504
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 68 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.45 Å3/Da / Density % sol: 49.72 %
Crystal growTemperature: 287 K / Method: vapor diffusion, hanging drop / Details: 0.1M Tris-HCl, pH 8.0, 3.5M sodium formate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.97852 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Sep 30, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97852 Å / Relative weight: 1
ReflectionResolution: 2.03→50 Å / Num. obs: 22500 / % possible obs: 100 % / Redundancy: 10.3 % / Net I/σ(I): 20.5

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Processing

Software
NameVersionClassification
REFMAC5.6.0117refinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.03→50 Å / Cor.coef. Fo:Fc: 0.923 / Cor.coef. Fo:Fc free: 0.888 / SU B: 14.694 / SU ML: 0.179 / Cross valid method: THROUGHOUT / ESU R Free: 0.226 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.29398 1068 5.1 %RANDOM
Rwork0.23344 ---
obs0.23657 19847 93.08 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 22.59 Å2
Baniso -1Baniso -2Baniso -3
1-0.07 Å20.03 Å20 Å2
2--0.07 Å20 Å2
3----0.1 Å2
Refinement stepCycle: 1 / Resolution: 2.03→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2536 0 0 68 2604
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0192571
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.621.9653486
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg9.3625343
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.07325.34103
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.27615444
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.161513
X-RAY DIFFRACTIONr_chiral_restr0.1150.2431
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0211881
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr5.35832571
X-RAY DIFFRACTIONr_sphericity_free37.52525
X-RAY DIFFRACTIONr_sphericity_bonded8.12152585
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A800.11
12C800.11
21B1100.1
22D1100.1
LS refinement shellResolution: 2.031→2.083 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.463 17 -
Rwork0.31 310 -
obs--19.7 %

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