4A2C

Crystal structure of galactitol-1-phosphate dehydrogenase from Escherichia coli

Summary for 4A2C

• Entry DOI: 10.2210/pdb4a2c/pdb
• Descriptor: GALACTITOL-1-PHOSPHATE 5-DEHYDROGENASE, NICKEL (II) ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase, metal binding-site
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 75167.03

Authors

Alvarez, Y.,Esteban-Torres, M.,Acebron, I.,de las Rivas, B.,Munoz, R.,Mancheno, J.M. (deposition date: 2011-09-26, release date: 2012-08-08, Last modification date: 2023-12-20)

Primary citation

Esteban-Torres, M.,Alvarez, Y.,Acebron, I.,De Las Rivas, B.,Munoz, R.,Kohring, G.-W.,Roa, A.M.,Sobrino, M.,Mancheno, J.M.
The Crystal Structure of Galactitol-1-Phosphate 5-Dehydrogenase from Escherichia Coli K12 Provides Insights Into its Anomalous Behavior on Imac Processes
FEBS Lett., 586:3127-, 2012

PubMed Abstract: 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.

PubMed: 22979983
DOI: 10.1016/J.FEBSLET.2012.07.073

Experimental method

X-RAY DIFFRACTION (1.87 Å)