ArticleBiophysical journal2007
Effects of serine-to-cysteine mutations on beta-lactamase folding.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 30 citations in OpenAlex.
- Predicting absolute protein folding stability using generative models.Protein science : a publication of the Protein Society · 2025Article
- Effect of Free Cysteine Residues to Serine Mutation on Cellodextrin Phosphorylase.Journal of applied glycoscience · 2024Article
- Fifty years of biophysics in Argentina.Biophysical reviews · 2023Article
- Identification and Functional Analysis of a Pseudo-Cysteine Protease from the Midgut Transcriptome ofInternational journal of molecular sciences · 2021Article
- Comparative Analysis of NADPH-Cytochrome P450 Reductases From Legumes for Heterologous Production of Triterpenoids in TransgenicFrontiers in plant science · 2021Article
- Gain-of-Function Mutations R249C and S250C in Complement C2 Protein Increase C3 Deposition in the Presence of C-Reactive Protein.Frontiers in immunology · 2021Article
- Equilibrium partially folded states of B. licheniformisEuropean biophysics journal : EBJ · 2019Article
- Global Implications of Local Unfolding Phenomena, Probed by Cysteine Reactivity in Human Frataxin.Scientific reports · 2019Article
- Impact of Mutations at Arg220 and Thr237 in PER-2 β-Lactamase on Conformation, Activity, and Susceptibility to Inhibitors.Antimicrobial agents and chemotherapy · 2017Article
- Increased genetic and phenotypic stability of a promising live-attenuated respiratory syncytial virus vaccine candidate by reverse genetics.Journal of virology · 2012Article
- X-ray evidence of a native state with increased compactness populated by tryptophan-less B. licheniformis β-lactamase.Protein science : a publication of the Protein Society · 2012Article
- A highly stable plastidic-type ferredoxin-NADP(H) reductase in the pathogenic bacterium Leptospira interrogans.PloS one · 2011Article
- The fast-folding HP35 double mutant has a substantially reduced primary folding free energy barrier.The Journal of chemical physics · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
B. licheniformis exo-small beta-lactamase (ESBL) has two nonsequential domains and a complex architecture. We replaced ESBL serine residues 126 and 265 with cysteine to probe the conformation of buried regions in each domain. Spectroscopic, hydrodynamic, and chemical methods revealed that the mutations do not alter the native fold but distinctly change stability (S-126C > wild-type > S-126/265C > S-265C ESBL) and the features of partially folded states. The observed wild-type ESBL equilibrium intermediate has decreased fluorescence but full secondary structure. S-126C ESBL intermediate has the fluorescence of the unfolded state, no thiol reactivity, and partial secondary structure. S-265C and S-126/265C ESBL populate intermediate states unfolded by fluorescence and thiol reactivity but with full secondary structure. Mass analysis of S-126/265C ESBL in the partially folded state proved that both thiol groups become exposed simultaneously. None of the intermediates is compatible with sequential domain unfolding. Molecular dynamics simulation suggests that the stabilizing effect of the S-126C substitution is due to optimization of van der Waals interactions and packing. On the other hand, destabilization induced by the S-265C mutation results from alteration of the hydrogen-bond network. The results illustrate the large impact that seemingly conservative serine-to-cysteine changes can have on the energy landscape of proteins.
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