SAXSdb — 8bvm

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

Catabolite repression control protein

Pseudomonas aeruginosa

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–RNA	Heteromer	Protein 15 RNA 1	RNA-binding protein Hfq × 12 （A6VD57） rbsB mRNA × 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	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–262； UniProt 1–259 Author chain H； PDBConstruct 4–262； UniProt 1–259 Author chain N； PDBConstruct 4–262； UniProt 1–259

RNA-binding protein Hfq

Pseudomonas aeruginosa

UniProt A6VD57

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–RNA	Heteromer	Protein 15 RNA 1	Catabolite repression control protein × 3 （Q51380） rbsB mRNA × 1	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HFQ_PSEA7
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–82； UniProt 1–82 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 G； PDBConstruct 1–82； UniProt 1–82 Author chain I； 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 O； PDBConstruct 1–82； UniProt 1–82

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_id	8bvm
Deposition date deposition_date	2022-12-04
Structure title title	Cryo-EM structure of Hfq-Crc-rbsB translation repression complex
Keywords keywords	;co-transcriptional RNA folding; Crc; metabolic regulation; ribonucleoprotein assembly; RNA chaperone Hfq; translational regulation, RNA BINDING PROTEIN ;; RNA BINDING PROTEIN
Experimental Method method	ELECTRON 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.

8bvm__assembly_1__model_1

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

Download this curve (.dat)

8bvm__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

8bvm__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	41.56 Å
Rg (electron density)	41.60 Å
Total Rg	41.76 Å
Atom count	13840
Residues	1630
Excluded volume	243780 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`8bvm__assembly_1__model_1`	hexadecameric （16）	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)

Entity 1 Entity 1 polymer

Description description	Catabolite repression control protein
Molecular weight formula_weight	30101.9 kDa
EC 编号 ec_number	3.1.11.2
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,H,N
Atom count atom_count	13918

GPAMRIISVNVNGIQAAAERGLLSWLQAQNADVICLQDTRASAFDLDDPSFQLDGYFLYACDAELPEQGGVALYSRLQPKAVISGLGFETADRYGRYLQADFDKVSIATLLLPSGQSGDESLNQKFKFMDDFTHYLSKQRRKRREYIYCGSLYVAHQKMDVKNWRECQQMPGFLAPERAWLDEVFGNLGYADALREVSREGDQFSWWPDSEQAEMLNLGWRFDYQVLTPGLRRFVRNAKLPRQPRFSQHAPLIVDYDWQLSI

Source Source

Source organism organism	Pseudomonas aeruginosa
NCBI taxonomy ID ncbi_taxonomy_id	287
Host organism host_organism	Pseudomonas aeruginosa

Entity 2 Entity 2 polymer

Description description	RNA-binding protein Hfq
Molecular weight formula_weight	9114.5 kDa
Source method src_method	man
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,C,D,E,F,G,I,J,K,L,M,O

MSKGHSLQDPYLNTLRKERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVRLPSGDQPAEPGNA

Source Source

Source organism organism	Pseudomonas aeruginosa
NCBI taxonomy ID ncbi_taxonomy_id	287
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	rbsB mRNA
Molecular weight formula_weight	34850.8 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polyribonucleotide
Chain IDs strand_id	u

AACGCAAACGUUUGCGUCUGGAUAAUCUCCUGGAAAAGAAUCAAUACAACGAUAAGAAAAGCUGGAGGAUAUACCAUGAAGCGGGUCGCUUCCCGGCGCCUGUUGGCU

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6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	8bvmN01
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	10 — Deoxyribonuclease I; Chain A
Homologous superfamily homologous superfamily	10 — Endonuclease/exonuclease/phosphatase

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.800 Å
Low-resolution limit resolution_low	3.800 Å
R factor r_factor	0.3993
R_work r_work	0.3993
R_free r_free	—

Resolution resolution	3.80 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	148700

Cryo-EM structure of Hfq-Crc-rbsB translation repression complex

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

Catabolite repression control protein

State in the Current Structure

Other States of the Same Protein in the Database

RNA-binding protein Hfq

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

8bvm__assembly_1__model_1

8bvm__assembly_1__model_1 | I(q)

8bvm__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)

Cryo-EM structure of Hfq-Crc-rbsB translation repression complex

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

Catabolite repression control protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

RNA-binding protein Hfq

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

8bvm__assembly_1__model_1

8bvm__assembly_1__model_1 | I(q)

8bvm__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)