› 4dxc

X-ray diffraction
2.3Å resolution

Crystal structure of the engineered MBP TEM-1 fusion protein RG13, C2 space group

Released:
DOI: 10.2210/pdb4dxc/pdb
PDB entry 4dxc coloured by chain, front view.
PDB entry 4dxc coloured by chain, side view.
PDB entry 4dxc coloured by chain, top view.
Source organisms:
Primary publication:
Structure of an engineered β-lactamase maltose binding protein fusion protein: insights into heterotropic allosteric regulation.
Ke W, Laurent AH, Armstrong MD, Chen Y, Smith WE, Liang J, Wright CM, Ostermeier M, van den Akker F
OpenAccess logo PLoS One 7 e39168 (2012)
PMID: 22720063

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142546 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase TEM; Maltose/maltodextrin-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 637 amino acids
Theoretical weight: 69.94 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 27-342, 343-385; Coverage: 97%)
  • Canonical: P62593 (Residues: 24-226, 228-270; Coverage: 93%)
Gene names: JW3994, b4034, bla, blaT-3, blaT-4, blaT-5, blaT-6, malE
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 124.45Å b: 47.844Å c: 108.288Å
α: 90° β: 114.14° γ: 90°
R-values:
R R work R free
0.236 0.233 0.291
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Engineering Allostery into Proteins.
Gorman et al. (2019)
1 more

5 mentions without citation

Design of protein switches based on an ensemble model of allostery.
Choi et al. (2015)
4 more