› 3ja6

Electron Microscopy
12.7Å resolution

Cryo-electron Tomography and All-atom Molecular Dynamics Simulations Reveal a Novel Kinase Conformational Switch in Bacterial Chemotaxis Signaling

Released:
DOI: 10.2210/pdb3ja6/pdb
PDB entry 3ja6 coloured by chain, front view.
PDB entry 3ja6 coloured by chain, side view.
PDB entry 3ja6 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
CryoEM and computer simulations reveal a novel kinase conformational switch in bacterial chemotaxis signaling.
Cassidy CK, Himes BA, Alvarez FJ, Ma J, Zhao G, Perilla JR, Schulten K, Zhang P
Elife 4 (2015)
PMID: 26583751
Related structures: EMD-6319

Function and Biology Details

Reaction catalysed: 
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero octadecamer (preferred)
PDBe Complex ID:
PDB-CPX-176353 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Chemotaxis protein CheW Chains: A, B, D, F
Molecule details ›
Chains: A, B, D, F
Length: 139 amino acids
Theoretical weight: 15.72 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q56311 (Residues: 9-147; Coverage: 92%)
Gene names: TM_0701, cheW
Sequence domains: CheW-like domain
Chemotaxis protein CheA Chains: C, E
Molecule details ›
Chains: C, E
Length: 379 amino acids
Theoretical weight: 42.49 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q56310 (Residues: 293-671; Coverage: 57%)
Gene names: TM_0702, cheA
Sequence domains:
Methyl-accepting chemotaxis protein 2 Chains: G, I, K, M, O, Q
Molecule details ›
Chains: G, I, K, M, O, Q
Length: 309 amino acids
Theoretical weight: 33.4 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0M7 (Residues: 222-529; Coverage: 58%)
Gene names: TM_1143, mcp2
Sequence domains: Methyl-accepting chemotaxis protein (MCP) signalling domain
Methyl-accepting chemotaxis protein 2 Chains: H, J, L, N, P, R
Molecule details ›
Chains: H, J, L, N, P, R
Length: 307 amino acids
Theoretical weight: 33.23 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0M7 (Residues: 222-528; Coverage: 58%)
Gene names: TM_1143, mcp2
Sequence domains: Methyl-accepting chemotaxis protein (MCP) signalling domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 12.7Å
Relevant EMDB volumes: EMD-6319
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Computational Methodologies for Real-Space Structural Refinement of Large Macromolecular Complexes.
Goh et al. (2016)
8 more

14 mentions without citation

CryoEM-based hybrid modeling approaches for structure determination.
Cassidy et al. (2018)
13 more