Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-12

AUTHORS

Martín E Noguera, Diego S Vazquez, Gerardo Ferrer-Sueta, William A Agudelo, Eduardo Howard, Rodolfo M Rasia, Bruno Manta, Alexandra Cousido-Siah, André Mitschler, Alberto Podjarny, Javier Santos

ABSTRACT

Thioredoxin is a ubiquitous small protein that catalyzes redox reactions of protein thiols. Additionally, thioredoxin from E. coli (EcTRX) is a widely-used model for structure-function studies. In a previous paper, we characterized several single-point mutants of the C-terminal helix (CTH) that alter global stability of EcTRX. However, spectroscopic signatures and enzymatic activity for some of these mutants were found essentially unaffected. A comprehensive structural characterization at the atomic level of these near-invariant mutants can provide detailed information about structural variability of EcTRX. We address this point through the determination of the crystal structures of four point-mutants, whose mutations occurs within or near the CTH, namely L94A, E101G, N106A and L107A. These structures are mostly unaffected compared with the wild-type variant. Notably, the E101G mutant presents a large region with two alternative traces for the backbone of the same chain. It represents a significant shift in backbone positions. Enzymatic activity measurements and conformational dynamics studies monitored by NMR and molecular dynamic simulations show that E101G mutation results in a small effect in the structural features of the protein. We hypothesize that these alternative conformations represent samples of the native-state ensemble of EcTRX, specifically the magnitude and location of conformational heterogeneity. More... »

PAGES

42343

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep42343

DOI

http://dx.doi.org/10.1038/srep42343

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1083736599

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28181556


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