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Domain motions in GroEL upon binding of an oligopeptide

X-ray diffraction
3Å resolution
PDB entry 1mnf coloured by chain, front view.
PDB entry 1mnf coloured by chain, side view.
PDB entry 1mnf coloured by chain, top view.
Source organism: Escherichia coli
Assembly composition:
hetero 28-mer (preferred)
Entry contents: 2 distinct polypeptide molecules

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Chaperonin GroEL and peptide
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Multimeric state: hetero 28-mer
Accessible surface area: 287646.8 Å2
Buried surface area: 70410.87 Å2
Dissociation area: 2,549.88 Å2
Dissociation energy (ΔGdiss): 8.04 kcal/mol
Dissociation entropy (TΔSdiss): 18.6 kcal/mol
Symmetry number: 14
PDBe Complex ID: PDB-CPX-141320

Macromolecules

Chaperonin GroEL
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 547 amino acids
Theoretical weight: 57.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 2-548; Coverage: 100%)
Gene names: JW4103, b4143, groEL, groL, mopA
Pfam: TCP-1/cpn60 chaperonin family
InterPro:
CATH:
SCOP:
Chaperonin GroEL in PDB entry 1mnf, assembly 1, front view.
Chaperonin GroEL in PDB entry 1mnf, assembly 1, side view.
Chaperonin GroEL in PDB entry 1mnf, assembly 1, top view.
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12-residue peptide substrate
Chains: 1, 2, O, P, Q, R, S, T, U, V, W, X, Y, Z
Length: 12 amino acids
Theoretical weight: 1.46 KDa
Source organism: Escherichia coli
Expression system: Not provided
12-residue peptide substrate in PDB entry 1mnf, assembly 1, front view.
12-residue peptide substrate in PDB entry 1mnf, assembly 1, side view.
12-residue peptide substrate in PDB entry 1mnf, assembly 1, top view.
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