1lb2

Structure of the E. coli alpha C-terminal domain of RNA polymerase in complex with CAP and DNA

Method: X-RAY DIFFRACTION Dmax: 85.4 Å Quality: EXCELLENT

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

CATABOLITE GENE ACTIVATOR PROTEIN

Escherichia coli

UniProt P0ACJ8

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 × 6 DNA 4 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 2–210 Not recorded 5'-D(*CP*TP*TP*TP*TP*TP*TP*CP*CP*TP*AP*AP*AP*AP*TP*GP*TP*GP*AP*T)-3' × 2 5'-D(*CP*TP*AP*GP*AP*TP*CP*AP*CP*AP*TP*TP*TP*TP*AP*GP*GP*AP*AP*AP*AP*AP*AP*G)-3' × 2 DNA-directed RNA polymerase alpha chain × 4 (P0A7Z4) CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;NaCl, NaAcetate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.10 Å R-free 0.244

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.

39 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRP_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–209; UniProt 2–210

DNA-directed RNA polymerase alpha chain

Escherichia coli

UniProt P0A7Z4

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 × 6 DNA 4 PDB declaration: decameric(10) Consistent with all polymer counts Chain B; UniProt 246–329 Chain E; UniProt 246–329 Fragment:alpha CTD, alpha Carboxy terminal domain 5'-D(*CP*TP*TP*TP*TP*TP*TP*CP*CP*TP*AP*AP*AP*AP*TP*GP*TP*GP*AP*T)-3' × 2 5'-D(*CP*TP*AP*GP*AP*TP*CP*AP*CP*AP*TP*TP*TP*TP*AP*GP*GP*AP*AP*AP*AP*AP*AP*G)-3' × 2 CATABOLITE GENE ACTIVATOR PROTEIN × 2 (P0ACJ8) CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;NaCl, NaAcetate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.10 Å R-free 0.244

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.

276 other PDB entries and 305 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–84; UniProt 246–329 Author chain E; PDBConstruct 1–84; UniProt 246–329

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 1lb2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1lb2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1lb2
Deposition date deposition_date2002-04-01
Structure title titleStructure of the E. coli alpha C-terminal domain of RNA polymerase in complex with CAP and DNA
Keywords keywordsPROTEIN-DNA COMPLEX, GENE-REGULATORY, GENE REGULATION-DNA COMPLEX; GENE REGULATION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.28
Radius of gyration Rg (electron density) rg_electron25.68
Forward intensity I(0) i059292700.00
Molecular weight molecular_weight51782.0 kDa
Excluded volume excluded_volume61439 ų
Envelope volume envelope_volume80661 ų
Hydration-shell volume shell_volume26979 ų
Envelope diameter envelope_diameter89.5
Shell Rg shell_rg32.01
Envelope Rg envelope_rg25.32
Shape Rg shape_rg25.71
Total Rg total_rg26.25
Total atoms total_atoms3581
Residues n_residues383
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 dmax85.4
Rg (real space) rg_real26.18
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real5.9290e+07
I(0) uncertainty (real space) i0_real_error9.0110e+05
Rg (reciprocal space) rg_reciprocal26.21
I(0) (reciprocal space) i0_reciprocal59290000.0000
Solution quality estimate total_estimate0.9013
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.2
Skewness Skewness skewness0.165
Kurtosis Kurtosis kurtosis-0.450
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3898000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1lb2a1
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.4 — CAP C-terminal domain-like
Domain ID domain_idd1lb2a2
Class classb — All beta proteins
Fold Fold foldb.82 — Double-stranded beta-helix
Superfamily Superfamily superfamilyb.82.3 — cAMP-binding domain-like
Family Family familyb.82.3.2 — cAMP-binding domain
Domain ID domain_idd1lb2b_
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.3 — C-terminal domain of RNA polymerase alpha subunit
Family Family familya.60.3.1 — C-terminal domain of RNA polymerase alpha subunit
Domain ID domain_idd1lb2e_
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.3 — C-terminal domain of RNA polymerase alpha subunit
Family Family familya.60.3.1 — C-terminal domain of RNA polymerase alpha subunit

CATH v4.4 (4 domains)

Domain ID domain_id1lb2A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
Domain ID domain_id1lb2A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Domain ID domain_id1lb2B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily20 — 5' to 3' exonuclease, C-terminal subdomain
Domain ID domain_id1lb2E00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily20 — 5' to 3' exonuclease, C-terminal subdomain

8. Citations (1)

9. Files and Curves (10)