X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism
| Autor: | L. A. Dadinova, Tatyana I. Nazarova, Natalia E. Snalina, Natalia N. Vorobyeva, S. A. Kurilova, Petr V. Konarev, E. V. Rodina, Eleonora V. Shtykova, Cy M. Jeffries, Dmitri I. Svergun |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Models Molecular Protein Conformation lcsh:Medicine Isomerase Protein Structure Prediction Biochemistry Physical Chemistry Small-Angle Scattering Scattering Mathematical and Statistical Techniques X-Ray Diffraction Fructose-Bisphosphate Aldolase Macromolecular Structure Analysis lcsh:Science Aldose-Ketose Isomerases chemistry.chemical_classification Multidisciplinary Crystallography biology Small-angle X-ray scattering Glutamate Decarboxylase Physics Protein structure prediction Condensed Matter Physics Enzyme structure Curve Fitting Solutions Chemistry Molecular Mass Inorganic Pyrophosphatase Physical Sciences Crystal Structure ddc:500 Research Article Protein Structure Materials by Structure Chemical physics Materials Science Research and Analysis Methods 03 medical and health sciences Scattering Small Angle Escherichia coli Solid State Physics Molecular Biology Inorganic pyrophosphatase 030102 biochemistry & molecular biology lcsh:R Aldolase A Biology and Life Sciences Proteins Computational Biology Dimers (Chemical physics) 030104 developmental biology Enzyme chemistry Structural biology Chemical Properties Oligomers Enzyme Structure biology.protein Biophysics Enzymology lcsh:Q Mathematical Functions |
| Zdroj: | PLoS ONE PLoS ONE, Vol 11, Iss 5, p e0156105 (2016) PLoS one 11(5), e0156105-(2016). doi:10.1371/journal.pone.0156105 |
| DOI: | 10.3204/pubdb-2017-00416 |
| Popis: | PLoS one 11(5), e0156105 -(2016). doi:10.1371/journal.pone.0156105 The structural analyses of four metabolic enzymes that maintain and regulate the stationary growth phase of Escherichia coli have been performed primarily drawing on the results obtained from solution small angle X-ray scattering (SAXS) and other structural techniques. The proteins are (i) class I fructose-1,6-bisphosphate aldolase (FbaB); (ii) inorganic pyrophosphatase (PPase); (iii) 5-keto-4-deoxyuronate isomerase (KduI); and (iv) glutamate decarboxylase (GadA). The enzyme FbaB, that until now had an unknown structure, is predicted to fold into a TIM-barrel motif that form globular protomers which SAXS experiments show associate into decameric assemblies. In agreement with previously reported crystal structures, PPase forms hexamers in solution that are similar to the previously reported X-ray crystal structure. Both KduI and GadA that are responsible for carbohydrate (pectin) metabolism and acid stress responses, respectively, form polydisperse mixtures consisting of different oligomeric states. Overall the SAXS experiments yield additional insights into shape and organization of these metabolic enzymes and further demonstrate the utility of hybrid methods, i.e., solution SAXS combined with X-ray crystallography, bioinformatics and predictive 3D-structural modeling, as tools to enrich structural studies. The results highlight the structural complexity that the protein components of metabolic networks may adopt which cannot be fully captured using individual structural biology techniques. Published by PLoS, Lawrence, Kan. |
| Databáze: | OpenAIRE |
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