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Manipulating the regioselectivity of phenylalanine aminomutase: new insights into the reaction mechanism of MIO-dependent enzymes from structure-guided directed evolution

X-ray diffraction
2.18Å resolution
PDB entry 2yii coloured by chain, front view.
PDB entry 2yii coloured by chain, side view.
PDB entry 2yii coloured by chain, top view.
Source organism: Taxus chinensis
Assembly composition:
homo tetramer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Phenylalanine aminomutase (L-beta-phenylalanine forming)
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Multimeric state: homo tetramer
Accessible surface area: 72004.89 Å2
Buried surface area: 38503.87 Å2
Dissociation area: 10,268.24 Å2
Dissociation energy (ΔGdiss): 139.68 kcal/mol
Dissociation entropy (TΔSdiss): 18.79 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-179344

Macromolecules

Phenylalanine aminomutase (L-beta-phenylalanine forming)
Chains: A, B, C, D
Length: 705 amino acids
Theoretical weight: 77.55 KDa
Source organism: Taxus chinensis
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: Q68G84 (Residues: 1-687; Coverage: 100%)
Gene name: pam
Pfam: Aromatic amino acid lyase
InterPro:
CATH:
Phenylalanine aminomutase (L-beta-phenylalanine forming) in PDB entry 2yii, assembly 1, front view.
Phenylalanine aminomutase (L-beta-phenylalanine forming) in PDB entry 2yii, assembly 1, side view.
Phenylalanine aminomutase (L-beta-phenylalanine forming) in PDB entry 2yii, assembly 1, top view.
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