publication . Article . 2017

Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis Acta Crystallographica Section D Structural Biology

Mills-Davies, N.; Butler, D.; Norton, E.; Thompson, D.; Sarwar, M.; Guo, J.; Gill, R.; Azim, N.; Coker, A.; Wood, S. P.; ...
Open Access
  • Published: 01 Jan 2017
  • Country: United Kingdom
Abstract
A number of X-ray analyses of an enzyme involved in a key early stage of tetrapyrrole biosynthesis are reported. Two structures of human 5-aminolaevulinate dehydratase (ALAD), native and recombinant, have been determined at 2.8 Å resolution, showing that the enzyme adopts an octameric quaternary structure in accord with previously published analyses of the enzyme from a range of other species. However, this is in contrast to the finding that a disease-related F12L mutant of the human enzyme uniquely forms hexamers [Breinig et al. (2003[Breinig, S., Kervinen, J., Stith, L., Wasson, A. S., Fairman, R., Wlodawer, A., Zdanov, A. & Jaffe, E. K. (2003). Nature Struct....
Subjects
free text keywords: Tetrapyrrole biosynthesis; chlorophyll; haem; 5-aminolaevulinic acid dehydratase; porphobilinogen synthase; protein crystallization; X-ray structure; TIM-barrel fold; thermostability; product complex
Download from
UCL Discovery
Article . 2017
87 references, page 1 of 6

Ajioka, R. S., Phillips, J. D. & Kushner, J. P. (2006). BBA 1763, 723-736.

Amo, T., Paje, M. L., Inagaki, A, Ezaki, S., Atomi, H. & Imanaka, T. (2002). Archaea. 1, 113-121.

Baker, N. A., Sept, D., Simpson, J., Holst, M. J. & McCammon, J. A. (2001). Proc. Natl. Acad. Sci.

USA 98, 10037-10041.

Bardag-Gorse, F. & French, S. W. (2011). Exp. Molec. Pathol. 91, 485-489.

Bevan, D. R., Bodlaender, P. & Shemin, D. (1980). J. Biol. Chem. 255, 2030-2035.

Boese, Q.F., Spano, A. J., Li, J. & Timko, M. P. (1991). J. Biol. Chem. 266, 17060-17066.

Breinig, S., Kervinen, J., Stith, L., Wasson, A. S., Fairman, R., Wlodawer, A., Zdanov, A. & Jaffe, E. K. (2003). Nat. Struct. Biol. 10, 757-763.

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, N., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T. & Warren, G. L. (1998). Acta Crystallogr. D 54, 905-921.

Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S. & Richardson, D. C. (2010). Acta Crystallogr. D 66, 12-21.

Coates, L., Beaven, G., Erskine, P. T., Beale, S. I., Avissar, Y. J., Gill, R., Mohammed, F., Wood, S. P., Shoolingin-Jordan, P. & Cooper, J. B. (2004). J. Molec. Biol. 342, 563-570.

Cooper, J. B. & Erskine, P. T. (2004). In 'Handbook of Metalloproteins. Vol. 3' Ed.

Messerschmidt, A., Bode, W. & Cygler, M. Wiley, Chichester, pp. 283-295.

Cowtan, K. (1994). Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography. 31, 34- 38.

Doss, M., Von-Tieperman, R., Schneider, J. and Schmid, H. (1979). Klin. Wochenschr. 57, 1123- 1127.

87 references, page 1 of 6
Abstract
A number of X-ray analyses of an enzyme involved in a key early stage of tetrapyrrole biosynthesis are reported. Two structures of human 5-aminolaevulinate dehydratase (ALAD), native and recombinant, have been determined at 2.8 Å resolution, showing that the enzyme adopts an octameric quaternary structure in accord with previously published analyses of the enzyme from a range of other species. However, this is in contrast to the finding that a disease-related F12L mutant of the human enzyme uniquely forms hexamers [Breinig et al. (2003[Breinig, S., Kervinen, J., Stith, L., Wasson, A. S., Fairman, R., Wlodawer, A., Zdanov, A. & Jaffe, E. K. (2003). Nature Struct....
Subjects
free text keywords: Tetrapyrrole biosynthesis; chlorophyll; haem; 5-aminolaevulinic acid dehydratase; porphobilinogen synthase; protein crystallization; X-ray structure; TIM-barrel fold; thermostability; product complex
Download from
UCL Discovery
Article . 2017
87 references, page 1 of 6

Ajioka, R. S., Phillips, J. D. & Kushner, J. P. (2006). BBA 1763, 723-736.

Amo, T., Paje, M. L., Inagaki, A, Ezaki, S., Atomi, H. & Imanaka, T. (2002). Archaea. 1, 113-121.

Baker, N. A., Sept, D., Simpson, J., Holst, M. J. & McCammon, J. A. (2001). Proc. Natl. Acad. Sci.

USA 98, 10037-10041.

Bardag-Gorse, F. & French, S. W. (2011). Exp. Molec. Pathol. 91, 485-489.

Bevan, D. R., Bodlaender, P. & Shemin, D. (1980). J. Biol. Chem. 255, 2030-2035.

Boese, Q.F., Spano, A. J., Li, J. & Timko, M. P. (1991). J. Biol. Chem. 266, 17060-17066.

Breinig, S., Kervinen, J., Stith, L., Wasson, A. S., Fairman, R., Wlodawer, A., Zdanov, A. & Jaffe, E. K. (2003). Nat. Struct. Biol. 10, 757-763.

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, N., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T. & Warren, G. L. (1998). Acta Crystallogr. D 54, 905-921.

Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S. & Richardson, D. C. (2010). Acta Crystallogr. D 66, 12-21.

Coates, L., Beaven, G., Erskine, P. T., Beale, S. I., Avissar, Y. J., Gill, R., Mohammed, F., Wood, S. P., Shoolingin-Jordan, P. & Cooper, J. B. (2004). J. Molec. Biol. 342, 563-570.

Cooper, J. B. & Erskine, P. T. (2004). In 'Handbook of Metalloproteins. Vol. 3' Ed.

Messerschmidt, A., Bode, W. & Cygler, M. Wiley, Chichester, pp. 283-295.

Cowtan, K. (1994). Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography. 31, 34- 38.

Doss, M., Von-Tieperman, R., Schneider, J. and Schmid, H. (1979). Klin. Wochenschr. 57, 1123- 1127.

87 references, page 1 of 6
Powered by OpenAIRE Open Research Graph
Any information missing or wrong?Report an Issue