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- PDB-1szv: Structure of the Adaptor Protein p14 reveals a Profilin-like Fold... -

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Basic information

Entry
Database: PDB / ID: 1szv
TitleStructure of the Adaptor Protein p14 reveals a Profilin-like Fold with Novel Function
ComponentsLate endosomal/lysosomal Mp1 interacting protein
KeywordsPROTEIN BINDING / P14
Function / homology
Function and homology information


Energy dependent regulation of mTOR by LKB1-AMPK / Amino acids regulate mTORC1 / MTOR signalling / Regulation of PTEN gene transcription / Macroautophagy / regulation of cell-substrate junction organization / TP53 Regulates Metabolic Genes / mTORC1-mediated signalling / FNIP-folliculin RagC/D GAP / Ragulator complex ...Energy dependent regulation of mTOR by LKB1-AMPK / Amino acids regulate mTORC1 / MTOR signalling / Regulation of PTEN gene transcription / Macroautophagy / regulation of cell-substrate junction organization / TP53 Regulates Metabolic Genes / mTORC1-mediated signalling / FNIP-folliculin RagC/D GAP / Ragulator complex / MAP2K and MAPK activation / protein localization to cell junction / TORC1 signaling / fibroblast migration / positive regulation of TOR signaling / positive regulation of TORC1 signaling / Neutrophil degranulation / guanyl-nucleotide exchange factor activity / regulation of cell growth / cellular response to amino acid stimulus / protein localization / late endosome / late endosome membrane / positive regulation of MAPK cascade / molecular adaptor activity / lysosomal membrane
Similarity search - Function
Ragulator complex protein LAMTOR2-like / Dynein light chain 2a, cytoplasmic / Roadblock/LAMTOR2 domain / Roadblock/LC7 domain / Roadblock/LC7 domain / Beta-Lactamase / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Ragulator complex protein LAMTOR2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / distance geometry, simulated annealing, molecular dynamics
AuthorsQian, C. / Zhang, Q. / Wang, X. / Zeng, L. / Farooq, A. / Zhou, M.M.
CitationJournal: J.Mol.Biol. / Year: 2005
Title: Structure of the Adaptor Protein p14 Reveals a Profilin-like Fold with Distinct Function
Authors: Qian, C. / Zhang, Q. / Wang, X. / Zeng, L. / Farooq, A. / Zhou, M.M.
History
DepositionApr 6, 2004Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Mar 15, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Late endosomal/lysosomal Mp1 interacting protein


Theoretical massNumber of molelcules
Total (without water)13,9021
Polymers13,9021
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 200structures with the lowest energy
RepresentativeModel #90lowest energy

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Components

#1: Protein Late endosomal/lysosomal Mp1 interacting protein / p14 / endosomal adaptor protein P14


Mass: 13901.878 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pGEX-6P-1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q9JHS3

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HNHA
121HN(CA)CB
131HN(CO)CA
141HN(CO)CACB
1514D 13C/15N-separated NOESY
NMR detailsText: This structure was determined using standard 3D heteronuclear techniques

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Sample preparation

Details
Solution-IDContentsSolvent system
10.3mM P14 U-15N,13C; 50mM phosphate90% H2O/10% D2O
20.3mM P14 U-15N,13C; 50mM phosphate100% D2O
30.3mM P14 U-2H,15N,13C; 50mM phosphate90% H2O/10% D2O
Sample conditionsIonic strength: 250mM NaCl / pH: 6.5 / Pressure: ambient / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX6001
Bruker DRXBrukerDRX5002
Bruker DPXBrukerDPX8003

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Processing

NMR softwareName: X-PLOR / Version: 3.1 / Developer: Brunger / Classification: refinement
RefinementMethod: distance geometry, simulated annealing, molecular dynamics
Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 1

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