Sanders' Lab Structure Gallery





UDP-galactose-4-epimerase from Aspergillus nidulans



Description : This work reported the crystal structure of UDP-galactose-4-epimerase from Aspergillus nidulans complexed with NAD and UDP-glucose. In addition, we examined the determinants of substrate specificity and used docking studies to rationalize the binding of UDP-galactose and UDP-N-acetyl-galactosamine.

Reference : PLoS One (2013) accepted August 29th, 2013. Dalrymple, S.A., Ko, J., Sheoran, I., Kaminskyj, S.G.W. and Sanders, D.A.R.


UDP-galactose-4-epimerase from Aspergillus nidulans complexed with NAD and UDP-glucose at 2.8 Å resolution. (GIF) (EDS)


IDH mutants designed to change cofactor specificity



Description : This work focused on trying to use protein engineering to alter the specificity of IDH from Bascillus subtilis from NADH to NADPH. In large part we were successful int his endeavour. The crystal structures of the double mutant A12K/D58S with and without NADP showed the NADPH bound, but with a surprising twisted conformation.

Reference : Biochemistry (2013) 52: 5876-5883. Zheng, H., Bertwistle, D., Sanders, D.A.R. and Palmer, D.R.J.


IDH mutant A12K/D58S from Bascillus subtilis at 1.95 Å resolution. (GIF) (EDS)
IDH mutant A12K/D58S from Bascillus subtilis complexed with NADP at 2.09 Å resolution. (GIF) (EDS)


UDP-galactopyranose Mutase from Aspergillus fumigatus



Description : This is the first reported structures of UGM from a eukaryotic pathogen. We have determined the crystal structures of UGM with and without substrates. Additionally, our crystal structures show rearrangements of the active site due to the oxidation state of the flavin cofactor. We have also determined the crystals structures of mutant UGMs with substrate bound.

Reference : J. Biol. Chem. (2012) 298: 10780-10790. van Straaten, K.E., Routier, F.H., and Sanders, D.A.R.


UDP-galactopyranose mutase from Aspergillus fumigatus at 2.64 Å resolution. (GIF) (EDS)
UDP-galactopyranose mutase from Aspergillus fumigatus with reduced FAD and complexed with UDP-Galp at 2.50 Å resolution. (GIF) (EDS)
UDP-galactopyranose mutase from Aspergillus fumigatus with oxidized FAD and complexed with UDP-Galp at 2.30 Å resolution. (GIF) (EDS)
UDP-galactopyranose mutase from Aspergillus fumigatus complexed with UDP at 2.63 Å resolution. (GIF) (EDS)
R182K mutant of UDP-galactopyranose mutase from Aspergillus fumigatus complexed with UDP-Galp at 2.75 Å resolution. (GIF) (EDS)
R327A mutant of UDP-galactopyranose mutase from Aspergillus fumigatus complexed with UDP-Galp at 3.10 Å resolution. (GIF) (EDS)
R327K mutant of UDP-galactopyranose mutase from Aspergillus fumigatus complexed with UDP-Galp at 3.15 Å resolution. (GIF) (EDS)


Inositol dehydrogenase from Bacillus subtilis



Description : Inositol dehydrogenase (IDH) catalyzes the conversion of 2-myo-Inositol to inosose, using NADH. We have determined the crystal structures of IDH with and without cofactor and substrate. We have also determined the crystals structures of an inactive mutant (K97V) with and without substrates/cofactors

Reference : Biochemical J. (2010) 432: 237-247. van Straaten, K.E., Zheng, H., Palmer, D.R.J., and Sanders, D.A.R.


Inositol dehydrogenase from Bacillus subtilis at 1.54 Å resolution. (GIF) (EDS)
Inositol dehydrogenase from Bacillus subtilis with bound cofactor at 2.30 Å resolution. (GIF) (EDS)
Inositol dehydrogenase from Bacillus subtilis with bound NADH and inositol at 2.50 Å resolution. (GIF) (EDS)
Inositol dehydrogenase from Bacillus subtilis with bound NAD and inosose at 2.90 Å resolution. (GIF) (EDS)
K97V mutant Inositol dehydrogenase from Bacillus subtilis at 1.91 Å resolution. (GIF) (EDS)
K97V mutant Inositol dehydrogenase from Bacillus subtilis with cofactor at 2.60 Å resolution. (GIF) (EDS)
K97V mutant Inositol dehydrogenase from Bacillus subtilis with cofactor and inositol at 2.65 Å resolution. (GIF) (EDS)


UDP-galactopyranose mutase from Deinococcus radiodurans complexed with the Phosphonate analogue of UDP-Galp



Description : This structure represents the first structure of UDP-galactopyranose mutase complexed with an inhibitor. The phosphonate analogue (anomeric oxygen replace with a carbon) is a poor inhibitor and the structure offers an explanation for this poor inhibition.

Reference : J. Mol. Biol. (2010) 403: 578-590. Karunan Partha, S., Sadeghi-Khomami, A., Slowski, K., Kotake, T. , Thomas, N.R. Jakeman, D.L. and Sanders, D.A.R.


UDP-galactopyranose mutase from Deinococcus radiodurans complexed with UDP-Phosphonate-Galp at 2.36 Å resolution. (GIF) (EDS)


Thioredoxin reductase from Deinococcus radiodurans



Description : Thioredoxin reductase is one of the proteins responsible for maintaining the proper redox state of the cytoplasm of cells. We have determiend the structure of TrxR and characterized its kinetic parameters. We have also examined the ability of the Trx system from D. radiodurans to interact with the E.coli Trx system.

Reference : J. Bacteriology (2010) 192: 494-501. Obiero, J., Pittet, V., Bonderoff, S.A. and Sanders, D.A.R.


Thioredoxin reductase from Deinococcus radiodurans at 1.9 Å resolution. (GIF) (EDS)


UDP-galactopyranose mutase from Deinococcus radiodurans



Description : UDP-galactopyranose mutase catalyzes an unprecedented interconversion of a 6 membered ring with a 5 membered ring. The product is an essential component of the cell wall of pathogenic micro-organisms, making this an ideal target for novel drug design. We have solved the structure of UGM complexed with substrates and with the flavin (FAD) oxidized and reduced.

Reference : J. Mol. Biol. (2009) 394: 864-877. Karunan Partha, S., van Straaten, K., Sanders, D.A.R.


UDP-galactopyranose mutase from Deinococcus radiodurans complexed with UDP-Galf and reduced FAD at 2.40 Å resolution. (GIF) (EDS)
UDP-galactopyranose mutase from Deinococcus radiodurans complexed with UDP at 2.40 Å resolution. (GIF) (EDS)
UDP-galactopyranose mutase from Deinococcus radiodurans complexed with UDP-Galf and oxidized FAD at 2.36 Å resolution. (GIF) (EDS)


Thioredoxin reductase from Helicobacter pylori



Description : Thioredoxin reductase is one of the proteins responsible for maintaining the proper redox state of the cytoplasm of cells.

Reference : Structure deposited October 2009. Obiero, J., van Straaten, K., Sanders, D.A.R.


Thioredoxin reductase from Helicobacter pylori at 2.43 Å resolution. (GIF) (EDS)


S-Formylglutathione Hydrolase from Agrobacterium tumefaciens



Description : S-Formylgutathione hydrolase catalyzes the cleavage of S-formylglutathione into formate and glutathione. This family of proteins is proposed to be part of the glutatione-dependent formadlehyde oxidation pathway. Unlike other members of this family, SFGH from A.tumifaciens shows a preference towards medium chain esters.

Reference : Protein Science (2009) 18: 2196-2202. van Straaten, K.E., Gonzalez, C.F., Valladares, R.B., Xu, X., Savchenko, A.V. and Sanders, D.A.R.


S-Formylglutathione Hydrolase from Agrobacterium tumefaciens at 2.01 Å resolution. (GIF) (EDS)


PA1607 from Pseudomonas aureginosa



Description : This small protein has an unknown function, but is similar to the MarR family of transcription regulators.

Reference : Protein Science (2007) 16: 543-549. Sieminska, E.A.L., Xu, X., Savchenko, A., and Sanders, D.A.R.


PA1607 from Pseudomonas aureginosa at 1.85 Å resolution. (GIF) (EDS)


PA3566 from Pseudomonas aureginosa



Description : This small protein has an unknown function, but is similar to small monooxygenases.

Reference : Proteins : Struct., Funct. & Bioinfo. (2005) 61: 209-212. Sanders, D.A.R., Walker, J.R., Skarina, T. and Savchenko, A.


PA3566 from Pseudomonas aureginosa at 1.78 Å resolution. (GIF) (EDS)