› 3lnr

X-ray diffraction
2.64Å resolution

Crystal structure of poly-HAMP domains from the P. aeruginosa soluble receptor Aer2

Released:
DOI: 10.2210/pdb3lnr/pdb
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Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Structure of concatenated HAMP domains provides a mechanism for signal transduction.
Airola MV, Watts KJ, Bilwes AM, Crane BR
Structure 18 436-48 (2010)
PMID: 20399181

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191472 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methyl-accepting chemotaxis protein McpB Chain: A
Molecule details ›
Chain: A
Length: 175 amino acids
Theoretical weight: 18.98 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9I6V6 (Residues: 1-172; Coverage: 25%)
Gene names: PA0176, aer-2, aer2, mcpB, tlpG
Sequence domains:
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)

Ligands and Environments

1 bound ligand:
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P43212
Unit cell:
a: 113.612Å b: 113.612Å c: 66.241Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.238 0.271
Expression system: Escherichia coli BL21(DE3)

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Citations

23 review citations

Signaling mechanisms of HAMP domains in chemoreceptors and sensor kinases.
Parkinson JS. (2010)
22 more

16 mentions without citation

Catalytically-active inclusion bodies for biotechnology-general concepts, optimization, and application.
Jäger et al. (2020)
15 more

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