› 3ah6

X-ray diffraction
2.4Å resolution

Remarkable improvement of the heat stability of CutA1 from E.coli by rational protein designing

Released:
DOI: 10.2210/pdb3ah6/pdb
PDB entry 3ah6 coloured by chain, front view.
PDB entry 3ah6 coloured by chain, side view.
PDB entry 3ah6 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Remarkable improvement in the heat stability of CutA1 from Escherichia coli by rational protein design.
Matsuura Y, Ota M, Tanaka T, Takehira M, Ogasahara K, Bagautdinov B, Kunishima N, Yutani K
J Biochem 148 449-58 (2010)
PMID: 20639520

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159595 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Divalent-cation tolerance protein CutA Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 112 amino acids
Theoretical weight: 12.35 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P69488 (Residues: 1-112; Coverage: 100%)
Gene names: JW4097, b4137, cutA, cutA1, cycY
Sequence domains: CutA1 divalent ion tolerance protein
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P212121
Unit cell:
a: 62.239Å b: 96.872Å c: 106.352Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.251
Expression system: Escherichia coli

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Citations

1 review citation

Differential scanning calorimetry as a tool for protein folding and stability.
Johnson CM. (2013)
5 other articles