Mapping the distribution of conformational information throughout a protein sequence

Journal of Molecular Biology
Leopoldo G GebhardMario R Ermácora

Abstract

The three-dimensional structure of protein is encoded in the sequence, but many amino acid residues carry no essential conformational information, and the identity of those that are structure-determining is elusive. By circular permutation and terminal deletion, we produced and purified 25 Bacillus licheniformis beta-lactamase (ESBL) variants that lack 5-21 contiguous residues each, and collectively have 82% of the sequence and 92% of the non-local atom-atom contacts eliminated. Circular dichroism and size-exclusion chromatography showed that most of the variants form conformationally heterogeneous mixtures, but by measuring catalytic constants, we found that all populate, to a greater or lesser extent, conformations with the essential features of the native fold. This suggests that no segment of the ESBL sequence is essential to the structure as a whole, which is congruent with the notion that local information and modular organization can impart most of the tertiary fold specificity and cooperativity.

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Citations

Jan 13, 2010·Journal of the American Chemical Society·Kannan R KarukurichiPhilip A Cole
Oct 10, 2008·Nucleic Acids Research·Wei-Cheng LoPing-Chiang Lyu
Jun 14, 2012·Nucleic Acids Research·Wei-Cheng LoPing-Chiang Lyu
Jan 24, 2009·Protein Science : a Publication of the Protein Society·Valeria A RissoMario R Ermácora
May 14, 2011·Biotechnology Journal·Bruno MantaAna Denicola
Apr 13, 2012·Protein Science : a Publication of the Protein Society·Valeria A RissoMario R Ermácora
Jun 22, 2010·Biophysical Chemistry·Valeria A RissoMario R Ermácora
May 15, 2007·Biophysical Journal·Javier SantosMario R Ermácora
Jul 24, 2014·Chemical Communications : Chem Comm·Hajin KimTae Hyeon Yoo
Apr 1, 2019·European Biophysics Journal : EBJ·Valeria A Risso, Mario R Ermácora
Aug 19, 2007·Biochemistry·Ravindra Singh PrajapatiRaghavan Varadarajan

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