YWHAB + ExoS: Human brain protein 14-3-3 beta isoform in complex with Exoenzyme S Peptide
PDB Code: 2C23
Phosphorylation of a target protein by a specific kinase alters the characteristics of the protein in a number of ways. One alteration is that the attached phosphate group presents a handle to which other molecules can bind thus forming a complex. This is generally how the 14-3-3 molecules interact with their proteins.
14-3-3 proteins are highly conserved eukaryotic proteins that bind to phosphorylated Ser (pS) residues via the two consensus sequences of RXXXpSXP and R(S/X)XpSXP. The functional unit is a dimer and their interaction with the phosphorylated target can result in stabilisation of the protein, alteration of enzyme activity, localisation within the cell, prevention of dephosphorylation and either blockage or mediation of protein interactions.
Previously the structure of the 14-3-3 proteins were believed to be rigid as the conformation of both the bound and unbound forms were essentially identical. This lead to the idea that the target proteins undergo a conformational change upon binding and that the 14-3-3 molecule remains unchanged. The apo-14-3-3beta crystal form (see webpage) revealed that the two monomers can adopt different conformations. Potentially the structural differences could be a result of the crystallisation process so to test this a known peptide that binds in the active site was soaked into the apo-14-3-3beta crystals to see if binding could induce a conformational change.
The first indication that a change had taken place was observed with a change in the crystal space group:

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