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Structure of a LAO-binding protein mutant with glutamineStructure of a LAO-binding protein mutant with glutamine
Structural highlights
FunctionARGT_SALTY This periplasmic binding protein is involved in an arginine transport system. ArgT and histidine-binding protein J (HisJ) interact with a common membrane-bound receptor, HisP. Publication Abstract from PubMedComputational protein design is still a challenge for advancing structure-function relationships. While recent advances in this field are promising, more information for genuine predictions is needed. Here, we discuss different approaches applied to install novel glutamine (Gln) binding into the Lysine/Arginine/Ornithine binding protein (LAOBP) from Salmonella typhimurium. We studied the ligand binding behaviour of two mutants: a binding pocket grafting design based on a structural superposition of LAOBP to the Gln binding protein QBP from Escherichia coli and a design based on statistical coupled positions. The latter showed the ability to bind Gln even though the protein was not very stable. Comparison of both approaches highlighted a non-conservative shared point mutation between LAOBP_graft and LAOBP_sca. This context dependent L117K mutation in LAOBP turned out to be sufficient for introducing Gln binding, as confirmed by different experimental techniques. Moreover, the crystal structure of LAOBP_L117K in complex with its ligand is reported. This article is protected by copyright. All rights reserved. Redesign of LAOBP to bind novel L-amino acid ligands.,Banda-Vazquez J, Shanmugaratnam S, Rodriguez-Sotres R, Torres-Larios A, Hocker B, Sosa-Peinado A Protein Sci. 2018 Mar 10. doi: 10.1002/pro.3403. PMID:29524280[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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