TEM1-beta-Lactamase/beta-lactamase Inhibitor Protein (BLIP)

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spinqualitylabelsall models PDB ID 1s0w Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The enzyme TEM1 and its protein inhibitor, form a . of the residues which participate in TEM1-BLIP interactions between: 1) complex of mutated BLIP (F142A) and wildtype TEM1 (lime; 1s0w); 2) complex of the wildtype BLIP/wildtype TEM1 (magenta; 1jtg); 3) unbound wildtype BLIP (structure from Ref 2) and unbound wildtype TEM1 (1btl), these two structures colored orange). T marks residues of TEM1 and B of BLIP. The distance between TEM Glu-104 and BLIP Lys-74 is marked for the wildtype (1jtg) and mutated (F142A, 1s0w) TEM1-BLIP complex structures (Refs 1, 2).

spinqualitylabelsall models PDB ID 1xxm Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The TEM1–BLIP in the KFYEY mutant structure (1xxm) is on the wildtype complex (1jtg) structure. Mutated TEM1 is shown in red, BLIP (lime) (1xxm) , wildtype TEM1 (yellow) and BLIP (1jtg) in orange, respectively. Mutated BLIP residues (K74A, F142A, Y143A) are colored in blue-violet, TEM1 residues E104 and Y105, where mutations to alanines were performed (i.g. E104A, Y105A), are colored blue and corresponding to them alanines A104 and A105 are colored magenta in the multiple mutant complex (KFYEY). These two structures are very similar. All-atom RMS deviation (RMSD) between the structures of the wildtype and the KFYEY mutant is 0.37 Å.

References

1) The modular architecture of protein-protein binding interfaces., Reichmann D, Rahat O, Albeck S, Meged R, Dym O, Schreiber G, Proc Natl Acad Sci U S A. 2005 Jan 4;102(1):57-62. Epub 2004 Dec 23. PMID:15618400

2) Structural and kinetic characterization of a beta-lactamase-inhibitor protein., Strynadka NC, Jensen S, Johns K, Blanchard H, Page M, Matagne A. et al., Nature 1994 Apr 14;368(6472):657-60. PMID: 8145854