1GTO: Hyperstable helical bundle protein mutant

High resolution structure of a hyperstable helical bundle protein mutant. Determined by X-ray diffraction at 1.82 Å resolution. Released 27 Jan 1997.

Method: X-ray diffraction
Resolution: 1.82 Å
Organism: Escherichia coli
Chains: 3
Atoms: 1,479
Mol. weight: 20.98 kDa
Released: 27 Jan 1997

Explore 1GTO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1GTO contains 6 α-helices and 0 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-28	27
α-helix	32-56	25

Chain B: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	4-28	25
α-helix	32-55	24

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	102-129	28
α-helix	132-156	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ROP	A, B, C	protein	62	Escherichia coli	P03051 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>1GTO_1 ROP (chains A, B, C)
GTKQEKTALNMARFIRSQTLTLLEKLNELGADEQADICESLHDHADELYRSCLARFGDDG
EN

Primary citation

Amino-acid substitutions in a surface turn modulate protein stability. Predki, P.F., Agrawal, V., Brunger, A.T. et al. Nat Struct Biol (1996) 3:54-58. DOI 10.1038/nsb0196-54 · PubMed

Other PDB entries of the same protein (UniProt P03051 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1NKD 1.09 Å, Atomic resolution (1.07 Å) structure of the rop mutant <2AA>
1RPO 1.4 Å, Restored heptad pattern continuity does not alter the folding of a 4-alpha-helical bundle
4DO2 1.4 Å, Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.
2IJK 1.55 Å, Structure of a Rom protein dimer at 1.55 angstrom resolution
7KAE 1.6 Å, Rop protein variant with a buried tryptophan
1ROP 1.7 Å, Structure of the COL*E1 rop protein at 1.7 Å resolution
1B6Q 1.8 Å, Alanine 31 proline mutant of rop protein
2IJH 1.8 Å, Crystal structure analysis of ColE1 ROM mutant F14W
1F4N 1.9 Å, C2 crystal structure of ALA2ILE2-6, a version of rop with a repacked hydrophobic core…
1GMG 1.9 Å, Alanine 31 proline mutant of rop protein, monoclinic form
2IJJ 1.9 Å, Crystal structure analysis of ColE1 ROM mutant F14Y
3K79 1.96 Å, C38A, C52V Cysteine-Free Variant of Rop (Rom)

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