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- PDB-4uem: UCH-L5 in complex with the RPN13 DEUBAD domain -

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Basic information

Entry
Database: PDB / ID: 4uem
TitleUCH-L5 in complex with the RPN13 DEUBAD domain
Components
  • PROTEASOMAL UBIQUITIN RECEPTOR ADRM1
  • UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5
KeywordsHYDROLASE / DEUBIQUITINATING ENZYME / DUB / PROTEASOME
Function / homology
Function and homology information


lateral ventricle development / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / forebrain morphogenesis / Ino80 complex / cytosolic proteasome complex / proteasome regulatory particle, lid subcomplex / positive regulation of smoothened signaling pathway / midbrain development / regulation of chromosome organization ...lateral ventricle development / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / forebrain morphogenesis / Ino80 complex / cytosolic proteasome complex / proteasome regulatory particle, lid subcomplex / positive regulation of smoothened signaling pathway / midbrain development / regulation of chromosome organization / endopeptidase inhibitor activity / molecular function inhibitor activity / proteasome binding / protein deubiquitination / regulation of DNA replication / regulation of embryonic development / endopeptidase activator activity / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / proteasome assembly / regulation of DNA repair / regulation of proteasomal protein catabolic process / positive regulation of DNA repair / telomere maintenance / proteasome complex / Downregulation of TGF-beta receptor signaling / transcription elongation by RNA polymerase II / UCH proteinases / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / DNA recombination / protease binding / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Ub-specific processing proteases / regulation of cell cycle / chromatin remodeling / DNA repair / nucleolus / positive regulation of DNA-templated transcription / RNA binding / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #860 / Ubiquitinyl hydrolase, UCH37 type / Ubiquitinyl hydrolase-L5 / Peptidase C12, C-terminal domain / Ubiquitin carboxyl-terminal hydrolases / RPN13, DEUBAD domain / RPN13, DEUBAD domain superfamily / UCH-binding domain / Ubiquitin C-terminal Hydrolase UCH-l3 / Peptidase C12, ubiquitin carboxyl-terminal hydrolase ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #860 / Ubiquitinyl hydrolase, UCH37 type / Ubiquitinyl hydrolase-L5 / Peptidase C12, C-terminal domain / Ubiquitin carboxyl-terminal hydrolases / RPN13, DEUBAD domain / RPN13, DEUBAD domain superfamily / UCH-binding domain / Ubiquitin C-terminal Hydrolase UCH-l3 / Peptidase C12, ubiquitin carboxyl-terminal hydrolase / DEUBAD domain / DEUBAD (DEUBiquitinase ADaptor) domain profile. / Peptidase C12, ubiquitin carboxyl-terminal hydrolase superfamily / Ubiquitin carboxyl-terminal hydrolase, family 1 / Peptidase C12, ubiquitin carboxyl-terminal hydrolase / Proteasomal ubiquitin receptor Rpn13/ADRM1 / Proteasomal ubiquitin receptor Rpn13/ADRM1, Pru domain superfamily / Rpn13/ADRM1, Pru domain / Proteasome complex subunit Rpn13, Pru domain / Pru (pleckstrin-like receptor for ubiquitin) domain profile. / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Papain-like cysteine peptidase superfamily / Up-down Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Proteasomal ubiquitin receptor ADRM1 / Ubiquitin carboxyl-terminal hydrolase isozyme L5
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.82 Å
AuthorsSahtoe, D.D. / Van Dijk, W.J. / El Oualid, F. / Ekkebus, R. / Ovaa, H. / Sixma, T.K.
CitationJournal: Mol.Cell / Year: 2015
Title: Mechanism of Uch-L5 Activation and Inhibition by Deubad Domains in Rpn13 and Ino80G.
Authors: Sahtoe, D.D. / Van Dijk, W.J. / El Oualid, F. / Ekkebus, R. / Ovaa, H. / Sixma, T.K.
History
DepositionDec 18, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 4, 2015Provider: repository / Type: Initial release
Revision 1.1Mar 25, 2015Group: Database references
Revision 1.2Apr 3, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval
Revision 1.3Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5
B: PROTEASOMAL UBIQUITIN RECEPTOR ADRM1


Theoretical massNumber of molelcules
Total (without water)50,8012
Polymers50,8012
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3720 Å2
ΔGint-34.9 kcal/mol
Surface area20250 Å2
MethodPISA
Unit cell
Length a, b, c (Å)56.596, 97.067, 100.616
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5 / UCH-L5 / UBIQUITIN C-TERMINAL HYDROLASE UCH37 / UBIQUITIN THIOESTERASE L5


Mass: 37734.934 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: ISOFORM 3 / Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PGEX-NKI-3C-LIC / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA 2 / References: UniProt: Q9Y5K5, ubiquitinyl hydrolase 1
#2: Protein PROTEASOMAL UBIQUITIN RECEPTOR ADRM1 / 110 KDA CELL MEMBRANE GLYCOPROTEIN / GP110 / ADHESION-REGULATING MOLECULE 1 / ARM-1 / PROTEASOME ...110 KDA CELL MEMBRANE GLYCOPROTEIN / GP110 / ADHESION-REGULATING MOLECULE 1 / ARM-1 / PROTEASOME REGULATORY PARTICLE NON-ATPASE 13 / HRPN13 / RPN13 HOMOLOG


Mass: 13065.674 Da / Num. of mol.: 1 / Fragment: DEUBAD DOMAIN, RESIDUES 266-388
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PCDF-NKI-HIS-3C-LIC / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA 2 / References: UniProt: Q16186
Sequence detailsISOFORM 3

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.7 Å3/Da / Density % sol: 54 % / Description: NONE
Crystal growTemperature: 277 K
Details: 100 MM BIS-TRIS-PROPANE PH 6.4, 230 MM NABR, 21% PEG3350. 4 DEGREES CELSIUS

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9793
DetectorType: ADSC CCD / Detector: CCD / Date: Jul 25, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 2.82→33.54 Å / Num. obs: 13635 / % possible obs: 98.5 % / Observed criterion σ(I): 2.2 / Redundancy: 3 % / Biso Wilson estimate: 77.01 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 15.3
Reflection shellResolution: 2.82→2.97 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.86 / Mean I/σ(I) obs: 2.2 / % possible all: 97.3

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3IHR

3ihr


Resolution: 2.82→28.853 Å / SU ML: 0.48 / σ(F): 1.34 / Phase error: 31.33 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2813 675 5 %
Rwork0.2318 --
obs0.234 13580 97.73 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.82→28.853 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2989 0 0 0 2989
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0033042
X-RAY DIFFRACTIONf_angle_d0.7354107
X-RAY DIFFRACTIONf_dihedral_angle_d12.7871146
X-RAY DIFFRACTIONf_chiral_restr0.028459
X-RAY DIFFRACTIONf_plane_restr0.003539
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8201-3.03760.3931520.33392507X-RAY DIFFRACTION97
3.0376-3.34290.38381510.30192558X-RAY DIFFRACTION99
3.3429-3.82570.27161220.2612571X-RAY DIFFRACTION99
3.8257-4.81630.30341230.21032622X-RAY DIFFRACTION98
4.8163-28.85450.22231270.20052647X-RAY DIFFRACTION95
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
14.99771.541-0.3286.2911-0.00486.2566-0.11630.2012-0.2359-0.39220.1416-0.36750.12450.1817-0.04140.55350.04140.01380.29420.0120.4088124.545691.0564122.3952
23.87181.3387-0.97313.7718-1.53155.35640.0488-0.4747-0.41250.5961-0.3436-0.69890.1180.81150.27060.4897-0.0136-0.12710.38830.04870.5745129.80889.1509129.1914
31.2098-0.53460.12710.71820.67761.5377-0.04190.02890.02140.14770.1343-0.0612-0.71980.3177-0.10920.838-0.1022-0.04360.4985-0.02040.5471133.5052112.008117.5688
40.15260.2605-0.31440.7112-0.68970.72990.10090.9682-1.1421-0.27070.2764-0.7508-0.28560.9580.06371.04020.08610.24951.26050.05161.1899155.3077108.424103.3493
56.53110.6597-0.28295.8579-1.41267.78230.2131-0.21920.15150.59140.022-0.8217-0.89611.3207-0.33370.6276-0.1402-0.13710.83630.06270.4897147.2903105.105494.8974
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 7:142)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 143:211)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 217:316)
4X-RAY DIFFRACTION4(CHAIN B AND RESID 287:297)
5X-RAY DIFFRACTION5(CHAIN B AND RESID 298:384)

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