8bvh

Cryo-EM structure of the Hfq-Crc-amiE translation repression assembly.

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

RNA-binding protein Hfq

Pseudomonas aeruginosa

UniProt A0A2V3F1A3

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–RNA Heteromer Protein 22 RNA 1 Catabolite repression control protein × 4 (Q51380) amiE × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0A2V3F1A3_PSEAI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–82; UniProt 1–82 Author chain D; PDBConstruct 1–82; UniProt 1–82 Author chain E; PDBConstruct 1–82; UniProt 1–82 Author chain F; PDBConstruct 1–82; UniProt 1–82 Author chain J; PDBConstruct 1–82; UniProt 1–82 Author chain K; PDBConstruct 1–82; UniProt 1–82 Author chain L; PDBConstruct 1–82; UniProt 1–82 Author chain M; PDBConstruct 1–82; UniProt 1–82 Author chain N; PDBConstruct 1–82; UniProt 1–82 Author chain O; PDBConstruct 1–82; UniProt 1–82 Author chain P; PDBConstruct 1–82; UniProt 1–82 Author chain Q; PDBConstruct 1–82; UniProt 1–82 Author chain R; PDBConstruct 1–82; UniProt 1–82 Author chain S; PDBConstruct 1–82; UniProt 1–82 Author chain T; PDBConstruct 1–82; UniProt 1–82 Author chain U; PDBConstruct 1–82; UniProt 1–82 Author chain w; PDBConstruct 1–82; UniProt 1–82 Author chain x; PDBConstruct 1–82; UniProt 1–82

Catabolite repression control protein

Pseudomonas aeruginosa

UniProt Q51380

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–RNA Heteromer Protein 22 RNA 1 RNA-binding protein Hfq × 18 (A0A2V3F1A3) amiE × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q51380_PSEAI
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–262; UniProt 1–259 Author chain G; PDBConstruct 4–262; UniProt 1–259 Author chain H; PDBConstruct 4–262; UniProt 1–259 Author chain I; PDBConstruct 4–262; UniProt 1–259

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id8bvh
Deposition date deposition_date2022-12-03
Structure title titleCryo-EM structure of the Hfq-Crc-amiE translation repression assembly.
Keywords keywords;co-transcriptional RNA folding; Crc; metabolic regulation; ribonucleoprotein assembly; RNA chaperone Hfq; translational regulation, RNA BINDING PROTEIN ;; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8bvh__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8bvh__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8bvh__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)43.44 Å
Rg (electron density)43.07 Å
Total Rg43.39 Å
Atom count38135
Residues2305
Excluded volume340620 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8bvh__assembly_1__model_1 23-meric (23) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8bvhB01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology10 — Deoxyribonuclease I; Chain A
Homologous superfamily homologous superfamily10 — Endonuclease/exonuclease/phosphatase
Domain ID domain_id8bvhG01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology10 — Deoxyribonuclease I; Chain A
Homologous superfamily homologous superfamily10 — Endonuclease/exonuclease/phosphatase
Domain ID domain_id8bvhH01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology10 — Deoxyribonuclease I; Chain A
Homologous superfamily homologous superfamily10 — Endonuclease/exonuclease/phosphatase
Domain ID domain_id8bvhI01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology10 — Deoxyribonuclease I; Chain A
Homologous superfamily homologous superfamily10 — Endonuclease/exonuclease/phosphatase
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7. Citations (1)