3erc

Crystal structure of the heterodimeric vaccinia virus mRNA polyadenylate polymerase with three fragments of RNA and 3'-deoxy ATP

Method: X-RAY DIFFRACTION Dmax: 129.8 Å Quality: GOOD

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

;Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase ;

vaccinia virus WR

UniProt P07617

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–RNA Heteromer Protein × 2 RNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 1–297 Mutation:R140A,K142A,R143A Poly(A) polymerase catalytic subunit × 1 (P23371) ;RNA/DNA chimera (5'-D(CP*)R(UP*UP*)D(CP*C)-3') ; × 1 ;RNA/DNA chimera (5'-D(CP*CP*)R(UP*UP*)D(C)-3') ; × 1 U5P URIDINE-5'-MONOPHOSPHATE × 1 3AT 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.7;295 K;Proteins(4-5mg.ml) in 10mM Tris-HCl, pH8.7, 75 mM NaCl, 0.5 mM DTT, mixed with equal volume buffer which composed of 10mM Tris-HCl, pH 8.7, 15-20% PEG 4000, 5% glycerol, 0.5 mM DTT. Room temperature for several days., VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.21 Å R-free 0.309
2 Protein–RNA Heteromer Protein × 2 RNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 1–297 Mutation:R140A,K142A,R143A Poly(A) polymerase catalytic subunit × 1 (P23371) ;RNA/DNA chimera (5'-D(CP*)R(UP*UP*)D(CP*C)-3') ; × 1 ;RNA/DNA chimera (5'-D(CP*)R(UP*UP*)-D(C)-3') ; × 1 U5P URIDINE-5'-MONOPHOSPHATE × 1 3AT 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.7;295 K;Proteins(4-5mg.ml) in 10mM Tris-HCl, pH8.7, 75 mM NaCl, 0.5 mM DTT, mixed with equal volume buffer which composed of 10mM Tris-HCl, pH 8.7, 15-20% PEG 4000, 5% glycerol, 0.5 mM DTT. Room temperature for several days., VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.21 Å R-free 0.309

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.

21 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAP2_VACCV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–297; UniProt 1–297 Author chain B; PDBConstruct 1–297; UniProt 1–297

Poly(A) polymerase catalytic subunit

vaccinia virus WR

UniProt P23371

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–RNA Heteromer Protein × 2 RNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain D; UniProt 1–479 Mutation:L36S ;Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase ; × 1 (P07617) ;RNA/DNA chimera (5'-D(CP*)R(UP*UP*)D(CP*C)-3') ; × 1 ;RNA/DNA chimera (5'-D(CP*CP*)R(UP*UP*)D(C)-3') ; × 1 U5P URIDINE-5'-MONOPHOSPHATE × 1 3AT 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.7;295 K;Proteins(4-5mg.ml) in 10mM Tris-HCl, pH8.7, 75 mM NaCl, 0.5 mM DTT, mixed with equal volume buffer which composed of 10mM Tris-HCl, pH 8.7, 15-20% PEG 4000, 5% glycerol, 0.5 mM DTT. Room temperature for several days., VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.21 Å R-free 0.309
2 Protein–RNA Heteromer Protein × 2 RNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain C; UniProt 1–479 Mutation:L36S ;Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase ; × 1 (P07617) ;RNA/DNA chimera (5'-D(CP*)R(UP*UP*)D(CP*C)-3') ; × 1 ;RNA/DNA chimera (5'-D(CP*)R(UP*UP*)-D(C)-3') ; × 1 U5P URIDINE-5'-MONOPHOSPHATE × 1 3AT 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.7;295 K;Proteins(4-5mg.ml) in 10mM Tris-HCl, pH8.7, 75 mM NaCl, 0.5 mM DTT, mixed with equal volume buffer which composed of 10mM Tris-HCl, pH 8.7, 15-20% PEG 4000, 5% glycerol, 0.5 mM DTT. Room temperature for several days., VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.21 Å R-free 0.309

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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAP1_VACCV
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–479; UniProt 1–479 Author chain D; PDBConstruct 1–479; UniProt 1–479

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 3erc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3erc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3erc
Deposition date deposition_date2008-10-01
Structure title titleCrystal structure of the heterodimeric vaccinia virus mRNA polyadenylate polymerase with three fragments of RNA and 3'-deoxy ATP
Keywords keywords;Polyadenylate polymerase, translocation, single tranded RNA poly(A) polymerase, RNA protein complex, processivity, heterodimer, nucleotidyltransferase, poxvirus; Methyltransferase, mRNA capping, mRNA processing, S-adenosyl-L-methionine, Transcription, Transferase, Transferase/DNA, RNA COMPLEX, Transferase-DNA ;; Transcription, Transferase/DNA, RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.07
Radius of gyration Rg (electron density) rg_electron38.74
Forward intensity I(0) i0463933000.00
Molecular weight molecular_weight178000.0 kDa
Excluded volume excluded_volume223570 ų
Envelope volume envelope_volume276390 ų
Hydration-shell volume shell_volume59523 ų
Envelope diameter envelope_diameter137.3
Shell Rg shell_rg44.44
Envelope Rg envelope_rg38.42
Shape Rg shape_rg38.72
Total Rg total_rg39.13
Total atoms total_atoms12479
Residues n_residues1485
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 dmax129.8
Rg (real space) rg_real39.16
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real4.6390e+08
I(0) uncertainty (real space) i0_real_error8.9990e+06
Rg (reciprocal space) rg_reciprocal39.11
I(0) (reciprocal space) i0_reciprocal463900000.0000
Solution quality estimate total_estimate0.8650
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.4
Skewness Skewness skewness0.435
Kurtosis Kurtosis kurtosis-0.183
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha200100000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.698

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id3ercA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39
Domain ID domain_id3ercB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39
Domain ID domain_id3ercC01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily320 — Poxvirus poly(A) polymerase, N domain
Domain ID domain_id3ercC03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology460 — Beta Polymerase; domain 2
Homologous superfamily homologous superfamily60 — Poxvirus poly(A) polymerase, nucleotidyltransferase domain
Domain ID domain_id3ercD01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily320 — Poxvirus poly(A) polymerase, N domain
Domain ID domain_id3ercD03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology460 — Beta Polymerase; domain 2
Homologous superfamily homologous superfamily60 — Poxvirus poly(A) polymerase, nucleotidyltransferase domain

8. Citations (2)

9. Files and Curves (10)