8hih

Cryo-EM structure of Mycobacterium tuberculosis transcription initiation complex with transcription factor GlnR

Method: ELECTRON MICROSCOPY Dmax: 194.7 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

DNA-directed RNA polymerase subunit alpha

Mycobacterium tuberculosis

UniProt P9WGZ1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain A; UniProt 1–347 Chain B; UniProt 1–347 Chain G; UniProt 1–347 Not recorded DNA-directed RNA polymerase subunit beta × 1 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) RNA polymerase sigma factor SigA × 1 (P9WGI1) Non-template strand DNA of amtB promoter × 1 Template strand DNA of amtB promoter × 1 Transcriptional regulatory protein × 4 (O53830) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.66 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

50 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_MYCTU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–347; UniProt 1–347 Author chain B; PDBConstruct 1–347; UniProt 1–347 Author chain G; PDBConstruct 1–347; UniProt 1–347

DNA-directed RNA polymerase subunit beta

Mycobacterium tuberculosis

UniProt P9WGY9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain C; UniProt 1–1178 Not recorded DNA-directed RNA polymerase subunit alpha × 3 (P9WGZ1) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) RNA polymerase sigma factor SigA × 1 (P9WGI1) Non-template strand DNA of amtB promoter × 1 Template strand DNA of amtB promoter × 1 Transcriptional regulatory protein × 4 (O53830) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.66 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

53 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOB_MYCTU
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1178; UniProt 1–1178

;DNA-directed RNA polymerase subunit beta' ;

Mycobacterium tuberculosis

UniProt P9WGY7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain D; UniProt 1–1316 Not recorded DNA-directed RNA polymerase subunit alpha × 3 (P9WGZ1) DNA-directed RNA polymerase subunit beta × 1 (P9WGY9) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) RNA polymerase sigma factor SigA × 1 (P9WGI1) Non-template strand DNA of amtB promoter × 1 Template strand DNA of amtB promoter × 1 Transcriptional regulatory protein × 4 (O53830) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.66 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

51 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOC_MYCTU
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–1316; UniProt 1–1316

DNA-directed RNA polymerase subunit omega

Mycobacterium tuberculosis H37Rv

UniProt P9WGY5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain E; UniProt 1–110 Not recorded DNA-directed RNA polymerase subunit alpha × 3 (P9WGZ1) DNA-directed RNA polymerase subunit beta × 1 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) RNA polymerase sigma factor SigA × 1 (P9WGI1) Non-template strand DNA of amtB promoter × 1 Template strand DNA of amtB promoter × 1 Transcriptional regulatory protein × 4 (O53830) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.66 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

46 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOZ_MYCTU
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–110; UniProt 1–110

RNA polymerase sigma factor SigA

Mycobacterium tuberculosis H37Rv

UniProt P9WGI1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain F; UniProt 1–528 Not recorded DNA-directed RNA polymerase subunit alpha × 3 (P9WGZ1) DNA-directed RNA polymerase subunit beta × 1 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) Non-template strand DNA of amtB promoter × 1 Template strand DNA of amtB promoter × 1 Transcriptional regulatory protein × 4 (O53830) ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.66 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIGA_MYCTU
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–528; UniProt 1–528

Transcriptional regulatory protein

Mycobacterium tuberculosis H37Rv

UniProt O53830

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 11 DNA 2 PDB declaration: tridecameric(13) Consistent with all polymer counts Chain N; UniProt 1–255 Chain O; UniProt 1–255 Chain P; UniProt 1–255 Chain Q; UniProt 1–255 Not recorded DNA-directed RNA polymerase subunit alpha × 3 (P9WGZ1) DNA-directed RNA polymerase subunit beta × 1 (P9WGY9) ;DNA-directed RNA polymerase subunit beta' ; × 1 (P9WGY7) DNA-directed RNA polymerase subunit omega × 1 (P9WGY5) RNA polymerase sigma factor SigA × 1 (P9WGI1) Non-template strand DNA of amtB promoter × 1 Template strand DNA of amtB promoter × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.66 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

1 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O53830_MYCTU
Isoform
PDB entities 8
Chains and sequence ranges Author chain N; PDBConstruct 1–255; UniProt 1–255 Author chain O; PDBConstruct 1–255; UniProt 1–255 Author chain P; PDBConstruct 1–255; UniProt 1–255 Author chain Q; PDBConstruct 1–255; UniProt 1–255

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8hih

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8hih
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8hih
Deposition date deposition_date2022-11-20
Structure title titleCryo-EM structure of Mycobacterium tuberculosis transcription initiation complex with transcription factor GlnR
Keywords keywordstranscription factor, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier57.45
Radius of gyration Rg (electron density) rg_electron56.64
Forward intensity I(0) i04063300000.00
Molecular weight molecular_weight501190.0 kDa
Excluded volume excluded_volume613610 ų
Envelope volume envelope_volume920400 ų
Hydration-shell volume shell_volume132060 ų
Envelope diameter envelope_diameter217.2
Shell Rg shell_rg61.61
Envelope Rg envelope_rg56.38
Shape Rg shape_rg56.62
Total Rg total_rg56.79
Total atoms total_atoms35064
Residues n_residues4317
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax194.7
Rg (real space) rg_real57.39
Rg uncertainty (real space) rg_real_error1.49
I(0) (real space) i0_real4.0630e+09
I(0) uncertainty (real space) i0_real_error7.8670e+07
Rg (reciprocal space) rg_reciprocal57.47
I(0) (reciprocal space) i0_reciprocal4064000000.0000
Solution quality estimate total_estimate0.6430
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary64.9
Skewness Skewness skewness0.348
Kurtosis Kurtosis kurtosis-0.259
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha445900000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 0.009; Positv: 1.000; Valcen: 0.998; Smooth: 0.839

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)