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- PDB-1do2: TRIGONAL CRYSTAL FORM OF HEAT SHOCK LOCUS U (HSLU) FROM ESCHERICH... -

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Basic information

Entry
Database: PDB / ID: 1do2
TitleTRIGONAL CRYSTAL FORM OF HEAT SHOCK LOCUS U (HSLU) FROM ESCHERICHIA COLI
ComponentsPROTEIN (HEAT SHOCK LOCUS U)
KeywordsCHAPERONE / HSLU / CLPY / AAA-ATPASE / ATP-DEPENDENT PROTEOLYSIS / PROTEASOME
Function / homology
Function and homology information


protein denaturation / HslUV protease complex / proteasome-activating activity / protein unfolding / proteolysis involved in protein catabolic process / cellular response to heat / peptidase activity / response to heat / protein domain specific binding / magnesium ion binding ...protein denaturation / HslUV protease complex / proteasome-activating activity / protein unfolding / proteolysis involved in protein catabolic process / cellular response to heat / peptidase activity / response to heat / protein domain specific binding / magnesium ion binding / ATP hydrolysis activity / proteolysis / ATP binding / membrane / identical protein binding / cytosol
Similarity search - Function
Heat shock protein HslU / Ubiquitin-associated (UBA) domain / Helicase, Ruva Protein; domain 3 - #60 / Clp ATPase, C-terminal / AAA domain (Cdc48 subfamily) / C-terminal, D2-small domain, of ClpB protein / C-terminal, D2-small domain, of ClpB protein / Helicase, Ruva Protein; domain 3 / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core ...Heat shock protein HslU / Ubiquitin-associated (UBA) domain / Helicase, Ruva Protein; domain 3 - #60 / Clp ATPase, C-terminal / AAA domain (Cdc48 subfamily) / C-terminal, D2-small domain, of ClpB protein / C-terminal, D2-small domain, of ClpB protein / Helicase, Ruva Protein; domain 3 / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / ATP-dependent protease ATPase subunit HslU
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4 Å
AuthorsBochtler, M. / Hartmann, C. / Song, H.K. / Bourenkov, G.P. / Bartunik, H.D.
Citation
Journal: Nature / Year: 2000
Title: The structures of HsIU and the ATP-dependent protease HsIU-HsIV.
Authors: Bochtler, M. / Hartmann, C. / Song, H.K. / Bourenkov, G.P. / Bartunik, H.D. / Huber, R.
#1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1997
Title: Crystal Structure of Heat Shock Locus V (HslV) from Escherichia coli
Authors: Bochtler, M. / Ditzel, L. / Groll, M. / Huber, R.
#2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1996
Title: HslV-HslU: A Novel ATP-Dependent Protease Complex in Escherichia coli Related to the Eukaryotic Proteasome
Authors: Rohrwild, M. / Coux, O. / Huang, H.C. / Moerschell, R.P. / Yoo, S.J. / Seol, J.H. / Chung, C.H. / Goldberg, A.L.
#3: Journal: Gene / Year: 1993
Title: Sequence Analysis of Four New Heat-Shock Genes Constituting the hslTS/ibpAB and hslVU Operons in Escherichia coli
Authors: Chuang, S.E. / Burland, V. / Plunket III, G. / Daniels, D.L. / Blattner, F.R.
History
DepositionDec 18, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 18, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Feb 7, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PROTEIN (HEAT SHOCK LOCUS U)
B: PROTEIN (HEAT SHOCK LOCUS U)
C: PROTEIN (HEAT SHOCK LOCUS U)
D: PROTEIN (HEAT SHOCK LOCUS U)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)199,1266
Polymers198,1144
Non-polymers1,0122
Water0
1
A: PROTEIN (HEAT SHOCK LOCUS U)
B: PROTEIN (HEAT SHOCK LOCUS U)
hetero molecules

A: PROTEIN (HEAT SHOCK LOCUS U)
B: PROTEIN (HEAT SHOCK LOCUS U)
hetero molecules

A: PROTEIN (HEAT SHOCK LOCUS U)
B: PROTEIN (HEAT SHOCK LOCUS U)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)298,6909
Polymers297,1716
Non-polymers1,5193
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_655-y+1,x-y,z1
crystal symmetry operation3_665-x+y+1,-x+1,z1
Buried area25040 Å2
ΔGint-98 kcal/mol
Surface area114790 Å2
MethodPISA, PQS
2
C: PROTEIN (HEAT SHOCK LOCUS U)
D: PROTEIN (HEAT SHOCK LOCUS U)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)99,5633
Polymers99,0572
Non-polymers5061
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area24280 Å2
ΔGint-87 kcal/mol
Surface area115080 Å2
MethodPISA
3
C: PROTEIN (HEAT SHOCK LOCUS U)
D: PROTEIN (HEAT SHOCK LOCUS U)
hetero molecules

C: PROTEIN (HEAT SHOCK LOCUS U)
D: PROTEIN (HEAT SHOCK LOCUS U)
hetero molecules

C: PROTEIN (HEAT SHOCK LOCUS U)
D: PROTEIN (HEAT SHOCK LOCUS U)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)298,6909
Polymers297,1716
Non-polymers1,5193
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-y+1,x-y+1,z1
crystal symmetry operation3_565-x+y,-x+1,z1
MethodPQS
Unit cell
Length a, b, c (Å)201.777, 201.777, 171.628
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number150
Space group name H-MP321

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Components

#1: Protein
PROTEIN (HEAT SHOCK LOCUS U)


Mass: 49528.508 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: XL-1 BLUE / Cellular location: CYTOPLASM / Plasmid: PET12B (T7 PROMOTOR) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P0A6H5
#2: Chemical ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER


Mass: 506.196 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H17N6O12P3 / Comment: AMP-PNP, energy-carrying molecule analogue*YM
Sequence detailsEDMAN-DEGRADATION HAS SHOWN THAT THE AMINOTERMINAL METHIONINE IS CLEAVED IN THE WILD TYPE. ...EDMAN-DEGRADATION HAS SHOWN THAT THE AMINOTERMINAL METHIONINE IS CLEAVED IN THE WILD TYPE. NEVERTHELESS, THIS METHIONINE RESIDUE HAS BEEN ASSIGNED RESIDUE NUMBER 1. THE FOLLOWING SERINE, THE FIRST RESIDUE OF THE MATURE PROTEIN, HAS BEEN ASSIGNED RESIDUE NUMBER 2 AN ENGINEERED VARIANT OF HSLU WITH THE SEVEN RESIDUE HIS-TAG, MHHHHHH, IN PLACE OF MET1 HAS BEEN USED FOR CRYSTALLIZATION. THIS TAG IS NOT CLEAVED IN THE MUTANT PROTEIN. AS THESE RESIDUES ARE NOT VISIBLE IN THE ELECTRON DENSITY, THEY HAVE BEEN OMITTED FROM THE MODEL.

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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: 5.09 Å3/Da / Density % sol: 75.84 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: reservoir: 100 mM sodium cacodylate, 15% glycerol, 10.5% PEG8000, 500 mM (NH4)2(SO4). drop: 0.002 ml reservoir solution, 0.002 ml 16 mg/ml protein in 20 mM Tris/HCl, pH 7.5, 5 mM MgCl2, 1 mM ...Details: reservoir: 100 mM sodium cacodylate, 15% glycerol, 10.5% PEG8000, 500 mM (NH4)2(SO4). drop: 0.002 ml reservoir solution, 0.002 ml 16 mg/ml protein in 20 mM Tris/HCl, pH 7.5, 5 mM MgCl2, 1 mM AMP-PNP, 1 mM NaN3, 0.0005 ml 1.0 M guanidinium chloride, 0.001 ml C12E8 , pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Crystal grow
*PLUS
Details: drop consists of equal volume of protein and reservoir solutions in Buffer B
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetailsChemical formula
116 mg/mlprotein1drop
220 mMTris-HCl1dropBuffer B
31 mMEDTA1dropBuffer B
41 mM1dropBuffer BNaN3
5100 mMsodium cacodylate1reservoir
615 %glycerol1reservoir
710.5 %PEG80001reservoir
8500 mMammonium sulfate1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MPG/DESY, HAMBURG / Beamline: BW6 / Wavelength: 1.0712
DetectorType: MARRESEARCH / Detector: CCD / Date: Jun 15, 1999 / Details: MIRROR
RadiationMonochromator: DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0712 Å / Relative weight: 1
ReflectionResolution: 4→20 Å / Num. all: 224179 / Num. obs: 32750 / % possible obs: 95.8 % / Redundancy: 6 % / Biso Wilson estimate: 50.4 Å2 / Rmerge(I) obs: 0.105 / Rsym value: 10.5
Reflection shellResolution: 4→4.07 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.337 / Rsym value: 33.7 / % possible all: 96.5
Reflection
*PLUS
Num. measured all: 224179
Reflection shell
*PLUS
% possible obs: 96.5 %

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Processing

Software
NameVersionClassification
AMoREphasing
X-PLOR3.851refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: HSLU FROM HSLU IN HSLVU CRYSTALS

Resolution: 4→15 Å / Rfactor Rfree error: 0.007 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
RfactorNum. reflection% reflectionSelection details
Rfree0.285 1611 5 %RANDOM
Rwork0.229 ---
obs0.229 32369 95.8 %-
Displacement parametersBiso mean: 50.4 Å2
Baniso -1Baniso -2Baniso -3
1--6.06 Å20.23 Å20 Å2
2---6.06 Å20 Å2
3---12.11 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.55 Å0.45 Å
Luzzati d res low-5 Å
Luzzati sigma a0.85 Å0.54 Å
Refinement stepCycle: LAST / Resolution: 4→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12864 0 62 0 12926
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONx_bond_d0.004
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_deg0.9
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d27
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d0.49
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it4.281.5
X-RAY DIFFRACTIONx_mcangle_it6.672
X-RAY DIFFRACTIONx_scbond_it11.972
X-RAY DIFFRACTIONx_scangle_it15.492.5
LS refinement shellResolution: 4→4.25 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.328 280 5.2 %
Rwork0.28 5066 -
obs--96.1 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PAPROTEIN.TOP
X-RAY DIFFRACTION2ANP.PARANP.TOP

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