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- PDB-6fdk: Structure of Chlamydia trachomatis effector protein Cdu1 bound to... -

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Basic information

Entry
Database: PDB / ID: 6fdk
TitleStructure of Chlamydia trachomatis effector protein Cdu1 bound to ubiquitin
Components
  • Deubiquitinase and deneddylase Dub1
  • Polyubiquitin-B
KeywordsHYDROLASE / ChlaDUB1 / CE protease / DUB / Ubiquitin.
Function / homology
Function and homology information


deNEDDylase activity / protein deneddylation / symbiont entry into host cell via disruption of host cell glycocalyx / symbiont entry into host cell via disruption of host cell envelope / virus tail / protein deubiquitination / host cell / cysteine-type deubiquitinase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / proteolysis ...deNEDDylase activity / protein deneddylation / symbiont entry into host cell via disruption of host cell glycocalyx / symbiont entry into host cell via disruption of host cell envelope / virus tail / protein deubiquitination / host cell / cysteine-type deubiquitinase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / proteolysis / extracellular region / membrane
Similarity search - Function
Ulp1 protease family, C-terminal catalytic domain / Ubiquitin-like protease family profile. / Ulp1 protease family, C-terminal catalytic domain / Pectate lyase superfamily protein / Rhamnogalacturonase A/epimerase, pectate lyase-like / Pectin lyase fold / Pectin lyase fold/virulence factor / Papain-like cysteine peptidase superfamily / Ubiquitin family
Similarity search - Domain/homology
prop-2-en-1-amine / Deubiquitinase and deneddylase Dub1 / Tail fiber
Similarity search - Component
Biological speciesChlamydia trachomatis 434/Bu (bacteria)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsRamirez, Y. / Kisker, C.
Funding support Germany, 1items
OrganizationGrant numberCountry
GSLS University of Wuerzburg Germany
CitationJournal: ChemMedChem / Year: 2018
Title: Structural Basis of Substrate Recognition and Covalent Inhibition of Cdu1 from Chlamydia trachomatis.
Authors: Ramirez, Y.A. / Adler, T.B. / Altmann, E. / Klemm, T. / Tiesmeyer, C. / Sauer, F. / Kathman, S.G. / Statsyuk, A.V. / Sotriffer, C. / Kisker, C.
History
DepositionDec 25, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 15, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 17, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 2.0Mar 15, 2023Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Polymer sequence / Source and taxonomy / Structure summary
Category: atom_site / database_2 ...atom_site / database_2 / entity / entity_poly / entity_poly_seq / entity_src_gen / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_unobs_or_zero_occ_residues / struct_conn / struct_ref / struct_ref_seq / struct_site
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.formula_weight / _entity_poly.nstd_monomer / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_src_gen.gene_src_common_name / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_scientific_name / _pdbx_nonpoly_scheme.pdb_seq_num / _pdbx_nonpoly_scheme.pdb_strand_id / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq.seq_align_end / _struct_site.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_seq_id
Revision 2.1Feb 7, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Deubiquitinase and deneddylase Dub1
B: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,0664
Polymers38,9742
Non-polymers932
Water7,620423
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2400 Å2
ΔGint-24 kcal/mol
Surface area14980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)47.815, 56.937, 60.695
Angle α, β, γ (deg.)90.00, 104.86, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Deubiquitinase and deneddylase Dub1 / ChlaDub1


Mass: 30454.164 Da / Num. of mol.: 1 / Mutation: C174A, C226S, C386A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chlamydia trachomatis 434/Bu (bacteria)
Gene: cdu1, CTL0247
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: B0B9A0, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases
#2: Protein Polyubiquitin-B


Mass: 8519.778 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P0CG47
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-AYE / prop-2-en-1-amine / ALLYLAMINE


Mass: 57.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H7N
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 423 / 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: 2.05 Å3/Da / Density % sol: 39.91 % / Description: Blade like
Crystal growTemperature: 293.15 K / Method: vapor diffusion, hanging drop / Details: 0.1 M MES pH 6.5, 12% PEG 20000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.98 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 20, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.6→46.22 Å / Num. obs: 41326 / % possible obs: 98.86 % / Redundancy: 6.7 % / Biso Wilson estimate: 23.74 Å2 / CC1/2: 0.999 / Rpim(I) all: 0.02739 / Rrim(I) all: 0.07178 / Net I/σ(I): 17.06
Reflection shellResolution: 1.6→1.657 Å / Redundancy: 7 % / Mean I/σ(I) obs: 1.32 / Num. unique obs: 4140 / CC1/2: 0.561 / Rpim(I) all: 0.6474 / % possible all: 99.9

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Processing

Software
NameVersionClassification
REFMAC5.8.0189refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5B5Q

5b5q


Resolution: 1.6→46.22 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.962 / SU B: 3.352 / SU ML: 0.07 / Cross valid method: FREE R-VALUE / ESU R: 0.092 / ESU R Free: 0.092 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20333 2021 4.9 %RANDOM
Rwork0.16955 ---
obs0.17122 39198 98.88 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 23.148 Å2
Baniso -1Baniso -2Baniso -3
1--0.12 Å20 Å20.35 Å2
2---0.19 Å20 Å2
3---0.12 Å2
Refinement stepCycle: 1 / Resolution: 1.6→46.22 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2543 0 5 423 2971
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.030.0192642
X-RAY DIFFRACTIONr_bond_other_d0.0030.022501
X-RAY DIFFRACTIONr_angle_refined_deg2.531.9723594
X-RAY DIFFRACTIONr_angle_other_deg1.28735833
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.2245324
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.69224.569116
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.16915473
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.0261513
X-RAY DIFFRACTIONr_chiral_restr0.190.2403
X-RAY DIFFRACTIONr_gen_planes_refined0.0140.0212881
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02517
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_it1.641.7781276
X-RAY DIFFRACTIONr_mcbond_other1.6381.7781275
X-RAY DIFFRACTIONr_mcangle_it2.3012.6651594
X-RAY DIFFRACTIONr_mcangle_other2.32.6651595
X-RAY DIFFRACTIONr_scbond_it3.0472.0911366
X-RAY DIFFRACTIONr_scbond_other3.0462.0911367
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.5442.9981996
X-RAY DIFFRACTIONr_long_range_B_refined6.37722.9522953
X-RAY DIFFRACTIONr_long_range_B_other6.37622.9482954
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.6→1.642 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.676 158 -
Rwork0.629 2895 -
obs--100 %
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)
10.91890.2247-0.00190.3147-0.02090.00990.00540.07720.0951-0.01190.00280.0218-0.00130.017-0.00820.05030.0034-0.00340.0396-0.00190.0132-6.1819-61.266373.2128
20.5858-0.05860.24680.1195-0.10680.16340.00950.0267-0.0284-0.0079-0.0033-0.0030.00970.0144-0.00620.04940.0089-0.00260.0266-0.00230.0018-3.8426-71.631871.0511
30.7425-0.52640.7170.489-0.38270.97080.0216-0.0272-0.09830.0130.0520.07860.0123-0.0266-0.07360.0358-0.0004-0.00830.03030.01170.0217-16.2645-77.32379.6119
40.79470.06940.0390.2925-0.14180.11850.063-0.01680.13550.0396-0.01130.0625-0.0119-0.007-0.05160.0510.01210.01760.00760.00280.0512-16.2576-56.846177.3477
500000000000000-00.0269000.026900.0269000
600000000000000-00.0269000.026900.0269000
700000000000000-00.0269000.026900.0269000
800000000000000-00.0269000.026900.0269000
900000000000000-00.0269000.026900.0269000
1000000000000000-00.0269000.026900.0269000
1100000000000000-00.0269000.026900.0269000
1200000000000000-00.0269000.026900.0269000
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A162 - 198
2X-RAY DIFFRACTION2A199 - 282
3X-RAY DIFFRACTION3A283 - 331
4X-RAY DIFFRACTION4A332 - 401
5X-RAY DIFFRACTION5B155 - 198
6X-RAY DIFFRACTION6B199 - 215
7X-RAY DIFFRACTION7B216 - 238
8X-RAY DIFFRACTION8B239 - 254
9X-RAY DIFFRACTION9B255 - 282
10X-RAY DIFFRACTION10B283 - 331
11X-RAY DIFFRACTION11B332 - 371
12X-RAY DIFFRACTION12B372 - 401

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