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- PDB-1atr: THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUC... -

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Entry
Database: PDB / ID: 1atr
TitleTHREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS
ComponentsHEAT-SHOCK COGNATE 70 KD PROTEIN
KeywordsCHAPERONE PROTEIN
Function / homologyHeat shock protein 70kD, peptide-binding domain superfamily / HSF1-dependent transactivation / Heat shock protein 70 family / Heat shock protein 70, conserved site / Heat shock protein 70kD, C-terminal domain superfamily / Hsp70 protein / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 3. / HSP90 chaperone cycle for steroid hormone receptors (SHR) ...Heat shock protein 70kD, peptide-binding domain superfamily / HSF1-dependent transactivation / Heat shock protein 70 family / Heat shock protein 70, conserved site / Heat shock protein 70kD, C-terminal domain superfamily / Hsp70 protein / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 3. / HSP90 chaperone cycle for steroid hormone receptors (SHR) / Attenuation phase / Regulation of HSF1-mediated heat shock response / Clathrin-mediated endocytosis / mRNA Splicing - Major Pathway / Golgi Associated Vesicle Biogenesis / Protein methylation / Lysosome Vesicle Biogenesis / AUF1 (hnRNP D0) binds and destabilizes mRNA / Neutrophil degranulation / synaptic vesicle uncoating / negative regulation of supramolecular fiber organization / chaperone-mediated protein transport involved in chaperone-mediated autophagy / clathrin-uncoating ATPase activity / slow axonal transport / chaperone-mediated autophagy translocation complex disassembly / protein targeting to lysosome involved in chaperone-mediated autophagy / late endosomal microautophagy / positive regulation by host of viral genome replication / postsynaptic specialization membrane / glycinergic synapse / C3HC4-type RING finger domain binding / chaperone complex / photoreceptor ribbon synapse / positive regulation of mRNA splicing, via spliceosome / presynaptic cytosol / regulation of postsynapse organization / Prp19 complex / axo-dendritic transport / misfolded protein binding / phosphatidylserine binding / autophagosome / protein folding chaperone / postsynaptic cytosol / ATP metabolic process / chaperone cofactor-dependent protein refolding / G protein-coupled receptor binding / ubiquitin ligase complex / spliceosomal complex / RNA splicing / cellular response to unfolded protein / vesicle-mediated transport / response to unfolded protein / heat shock protein binding / ATPase activity, coupled / regulation of cell cycle / protein binding, bridging / terminal bouton / mRNA processing / regulation of protein stability / ribonucleoprotein complex / melanosome / late endosome / unfolded protein binding / cellular response to heat / chaperone binding / lysosome / protein refolding / ATPase activity / myelin sheath / axon / glutamatergic synapse / dendrite / negative regulation of transcription, DNA-templated / nucleolus / ubiquitin protein ligase binding / perinuclear region of cytoplasm / extracellular exosome / ATP binding / plasma membrane / nucleus / cytosol / cytoplasm / Heat shock cognate 71 kDa protein
Function and homology information
Specimen sourceBos taurus (cattle)
MethodX-RAY DIFFRACTION / 2.34 Å resolution
AuthorsO'Brien, M.C. / Mckay, D.B.
Citation
Journal: J.Biol.Chem. / Year: 1993
Title: Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis.
Authors: O'Brien, M.C. / McKay, D.B.
#1: Journal: Nature / Year: 1990
Title: Three-Dimensional Structure of the ATPase Fragment of a 70K Heat-Shock Cognate Protein
Authors: Flaherty, K.M. / De Luca-Flaherty, C. / Mckay, D.B.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Aug 9, 1993 / Release: Oct 31, 1993
RevisionDateData content typeGroupProviderType
1.0Oct 31, 1993Structure modelrepositoryInitial release
1.1Mar 24, 2008Structure modelVersion format compliance
1.2Jul 13, 2011Structure modelVersion format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: HEAT-SHOCK COGNATE 70 KD PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0584
Polyers42,5111
Non-polymers5463
Water2,090116
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)145.300, 65.000, 46.900
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP 21 21 21

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Components

#1: Protein/peptide HEAT-SHOCK COGNATE 70 KD PROTEIN


Mass: 42511.062 Da / Num. of mol.: 1 / Source: (gene. exp.) Bos taurus (cattle) / Genus: Bos / Organ: BRAIN / References: UniProt: P19120, adenosinetriphosphatase
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Formula: Mg / Magnesium
#3: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 1 / Formula: PO4 / Phosphate
#4: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 1 / Formula: C10H15N5O10P2 / Adenosine diphosphate / Comment: ADP (energy-carrying molecule) *YM
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 116 / Formula: H2O / Water

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.6 / Density percent sol: 52.77 %
Crystal grow
*PLUS
pH: 9 / Method: other
components of the solutions
*PLUS
IDConcCommon nameCrystal IDSol IDChemical formula
120 %PEG80001reservoir
21 M1reservoirNaCl

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
D resolution high: 2.1 Å / Number obs: 16797 / Number all: 14417 / Rmerge I obs: 0.031

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
Least-squares processR factor R work: 0.218 / R factor obs: 0.218 / Highest resolution: 2.34 Å / Number reflection obs: 1
Refine hist #LASTHighest resolution: 2.34 Å
Number of atoms included #LASTProtein: 2965 / Nucleic acid: 0 / Ligand: 33 / Solvent: 116 / Total: 3114
Refine LS restraints
Refine IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.007
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.43
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Software
*PLUS
Name: X-PLOR / Classification: refinement
Least-squares process
*PLUS
R factor obs: 0.218 / Highest resolution: 2.34 Å / Number reflection obs: 16797
Refine LS restraints
*PLUS
Type: x_angle_d / Dev ideal: 1.43

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