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8AG8

Structure of the Fluorescence Recovery-like protein FRPL from Pseudomonas borbori

Summary for 8AG8
Entry DOI10.2210/pdb8ag8/pdb
DescriptorFluorescence Recovery-like protein, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID (3 entities in total)
Functional Keywordsstress-related, alpha-helical bundle, dimer, protein binding
Biological sourcePseudomonas borbori
Total number of polymer chains1
Total formula weight13610.59
Authors
Weiland, P.,Bange, G. (deposition date: 2022-07-19, release date: 2023-04-05, Last modification date: 2024-02-07)
Primary citationSteube, N.,Moldenhauer, M.,Weiland, P.,Saman, D.,Kilb, A.,Ramirez Rojas, A.A.,Garg, S.G.,Schindler, D.,Graumann, P.L.,Benesch, J.L.P.,Bange, G.,Friedrich, T.,Hochberg, G.K.A.
Fortuitously compatible protein surfaces primed allosteric control in cyanobacterial photoprotection.
Nat Ecol Evol, 7:756-767, 2023
Cited by
PubMed Abstract: Highly specific interactions between proteins are a fundamental prerequisite for life, but how they evolve remains an unsolved problem. In particular, interactions between initially unrelated proteins require that they evolve matching surfaces. It is unclear whether such surface compatibilities can only be built by selection in small incremental steps, or whether they can also emerge fortuitously. Here, we used molecular phylogenetics, ancestral sequence reconstruction and biophysical characterization of resurrected proteins to retrace the evolution of an allosteric interaction between two proteins that act in the cyanobacterial photoprotection system. We show that this interaction between the orange carotenoid protein (OCP) and its unrelated regulator, the fluorescence recovery protein (FRP), evolved when a precursor of FRP was horizontally acquired by cyanobacteria. FRP's precursors could already interact with and regulate OCP even before these proteins first encountered each other in an ancestral cyanobacterium. The OCP-FRP interaction exploits an ancient dimer interface in OCP, which also predates the recruitment of FRP into the photoprotection system. Together, our work shows how evolution can fashion complex regulatory systems easily out of pre-existing components.
PubMed: 37012377
DOI: 10.1038/s41559-023-02018-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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