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Título: | The crystal structure of galactitol-1-phosphate 5-dehydrogenase from Escherichia coli K12 provides insights into its anomalous behavior on IMAC processes |
Autor: | Esteban-Torres, María CSIC ORCID; Álvarez, Yanaisis CSIC; Acebrón, Iván CSIC ORCID; Rivas, Blanca de las CSIC ORCID; Muñoz, Rosario CSIC ORCID ; Kohring, G. W.; Roa, A. M.; Sobrino, M.; Mancheño, Jose M. CSIC ORCID | Fecha de publicación: | 21-sep-2012 | Editor: | John Wiley & Sons | Citación: | FEBS Letters 586(19): 3127-3133 (2012) | Resumen: | Endogenous galactitol-1-phosphate 5-dehydrogenase (GPDH) (EC 1.1.1.251) from Escherichia coli spontaneously interacts with Ni 2+-NTA matrices becoming a potential contaminant for recombinant, target His-tagged proteins. Purified recombinant, untagged GPDH (rGPDH) converted galactitol into tagatose, and d-tagatose-6-phosphate into galactitol-1-phosphate, in a Zn 2+- and NAD(H)-dependent manner and readily crystallized what has permitted to solve its crystal structure. In contrast, N-terminally His-tagged GPDH was marginally stable and readily aggregated. The structure of rGPDH revealed metal-binding sites characteristic from the medium-chain dehydrogenase/reductase protein superfamily which may explain its ability to interact with immobilized metals. The structure also provides clues on the harmful effects of the N-terminal His-tag. Structured summary of protein interactions: GPDH and GPDH bind by molecular sieving (View interaction) GPDH and GPDH bind by x-ray crystallography (View interaction) GPDH and GPDH bind by cosedimentation in solution (View interaction). © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | Versión del editor: | http://dx.doi.org/10.1016/j.febslet.2012.07.073 | URI: | http://hdl.handle.net/10261/67296 | DOI: | 10.1016/j.febslet.2012.07.073 | Identificadores: | issn: 0014-5793 |
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