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- PDB-6pj9: Time-resolved structural snapshot of proteolysis by GlpG inside t... -

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Basic information

Entry
Database: PDB / ID: 6pj9
TitleTime-resolved structural snapshot of proteolysis by GlpG inside the membrane
Components
  • Peptide aldehyde inhibitor
  • Rhomboid protease GlpG
KeywordsMEMBRANE PROTEIN / inhibitor
Function / homology
Function and homology information


maternal determination of dorsal/ventral axis, ovarian follicular epithelium, germ-line encoded / dorsal/ventral axis specification, ovarian follicular epithelium / anterior/posterior axis specification, follicular epithelium / determination of dorsal identity / chorion-containing eggshell pattern formation / oocyte anterior/posterior axis specification / oocyte microtubule cytoskeleton organization / oocyte dorsal/ventral axis specification / imaginal disc-derived wing vein specification / dorsal appendage formation ...maternal determination of dorsal/ventral axis, ovarian follicular epithelium, germ-line encoded / dorsal/ventral axis specification, ovarian follicular epithelium / anterior/posterior axis specification, follicular epithelium / determination of dorsal identity / chorion-containing eggshell pattern formation / oocyte anterior/posterior axis specification / oocyte microtubule cytoskeleton organization / oocyte dorsal/ventral axis specification / imaginal disc-derived wing vein specification / dorsal appendage formation / positive regulation of border follicle cell migration / rhomboid protease / epidermal growth factor receptor binding / anterior/posterior pattern specification / epidermal growth factor receptor signaling pathway / endopeptidase activity / cell surface receptor signaling pathway / receptor ligand activity / serine-type endopeptidase activity / proteolysis / extracellular space / identical protein binding / plasma membrane
Similarity search - Function
Protein Gurken/Spitz / Rhomboid-like fold / Rhomboid-like / Peptidase S54, GlpG peptidase, N-terminal / Rhomboid protease GlpG / GlpG peptidase, N-terminal domain superfamily / Cytoplasmic N-terminal domain of rhomboid serine protease / Peptidase S54, rhomboid domain / Rhomboid family / Rhomboid-like superfamily ...Protein Gurken/Spitz / Rhomboid-like fold / Rhomboid-like / Peptidase S54, GlpG peptidase, N-terminal / Rhomboid protease GlpG / GlpG peptidase, N-terminal domain superfamily / Cytoplasmic N-terminal domain of rhomboid serine protease / Peptidase S54, rhomboid domain / Rhomboid family / Rhomboid-like superfamily / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Rhomboid protease GlpG / Rhomboid protease GlpG / Protein gurken
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Drosophila melanogaster (fruit fly)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsUrban, S. / Cho, S.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)R01AI066025 United States
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2019
Title: Ten catalytic snapshots of rhomboid intramembrane proteolysis from gate opening to peptide release.
Authors: Cho, S. / Baker, R.P. / Ji, M. / Urban, S.
History
DepositionJun 28, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 2, 2019Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2019Group: Data collection / Database references / Category: citation / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Nov 27, 2019Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Dec 18, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Oct 11, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Rhomboid protease GlpG
B: Peptide aldehyde inhibitor


Theoretical massNumber of molelcules
Total (without water)24,2772
Polymers24,2772
Non-polymers00
Water21612
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area930 Å2
ΔGint-6 kcal/mol
Surface area9190 Å2
MethodPISA
Unit cell
Length a, b, c (Å)71.260, 99.000, 63.210
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221

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Components

#1: Protein Rhomboid protease GlpG / Intramembrane serine protease


Mass: 23800.133 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: glpG, APT88_21985, SK83_00858 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3)
References: UniProt: A0A0J2E248, UniProt: P09391*PLUS, rhomboid protease
#2: Protein/peptide Peptide aldehyde inhibitor


Mass: 476.613 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Drosophila melanogaster (fruit fly) / References: UniProt: P42287*PLUS
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 12 / 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: 2.2 Å3/Da / Density % sol: 44.12 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop
Details: 0.1 M Na-acetate pH 5.5, 3 M NaCl, and 5 % ethylene glycol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.979 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Jun 20, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.5→57.84 Å / Num. obs: 7975 / % possible obs: 99.2 % / Redundancy: 3.9 % / Rsym value: 0.089 / Net I/σ(I): 4.5
Reflection shellResolution: 2.5→2.6 Å / Num. unique obs: 871 / Rsym value: 0.687

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Processing

Software
NameVersionClassification
REFMAC5.8.0230refinement
iMOSFLMdata reduction
Aimlessdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5F5D

5f5d


Resolution: 2.5→57.84 Å / Cor.coef. Fo:Fc: 0.911 / Cor.coef. Fo:Fc free: 0.918 / SU B: 21.361 / SU ML: 0.397 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.6 / ESU R Free: 0.314 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2807 375 4.7 %RANDOM
Rwork0.2576 ---
obs0.2587 7588 99.18 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 129.21 Å2 / Biso mean: 60.176 Å2 / Biso min: 29.12 Å2
Baniso -1Baniso -2Baniso -3
1-10.14 Å2-0 Å20 Å2
2---5.21 Å20 Å2
3----4.93 Å2
Refinement stepCycle: final / Resolution: 2.5→57.84 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1430 0 0 12 1442
Biso mean---48 -
Num. residues----180
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0121476
X-RAY DIFFRACTIONr_angle_refined_deg1.4731.5912006
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.5755177
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.23320.95263
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.83715229
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.359156
X-RAY DIFFRACTIONr_chiral_restr0.1320.2178
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.021089
LS refinement shellResolution: 2.5→2.565 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.442 21 -
Rwork0.397 551 -
all-572 -
obs--99.31 %

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