How are charged residues distributed among functionally distinct structural domains of aminoacyl-tRNA synthetases?

Mark Safro, Dmitry Tworowski, Anna Feldman

Research output: Contribution to journalConference articlepeer-review

Abstract

Motivation: Unlike many other families of enzymes, which catalyze the same overall reaction, aminoacyl-tRNA synthetases (aaRSs) are extremely heterogeneous in terms of primary sequence and subunit organization. For the most part aaRSs are negatively charged at physiological conditions, as are tRNA substrates. What are the driving forces that ensure an attraction between like-charged macromolecules? As may be inferred from multiple sequence alignments (MSA), concentration of the invariant charged residues in structural domains doesn't correlate with contribution of the domains to formation of the electrostatic field at long distances. Results: In aaRSs family the subset of evolutionary non-conserved charged residues generates long-range electrostatic potential (EP) similar to the native one. We evaluate contribution of individual structural domains to the EP generated by native (NS), conservative (CS) and non-conservative subsets (NCS) of charged residues. For monomeric IIeRS and heterodimeric PheRS we further analyzed the interplay between the domain functionality and their role in the field formation at long distances.
Original languageEnglish
Pages (from-to)310-314
Number of pages5
JournalProceedings Of The Fifth International Conference On Bioinformatics Of Genome Regulation And Structure, Vol 1
Publication statusPublished - 2006
Event5th International Conference on Bioinformatics of Genome Regulation and Structure - Novosibirsk, RUSSIA
Duration: 16 Jul 200622 Jul 2006

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