Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: Tetrahydromethanopterin formyltransferase from Methanopyrus kandleri

Proteins: Structure, Function and Genetics

Volumn 26, Issue 1, 1996, Pages 118-120

  Shima, Seigo ^a   Thauer, Rudolf K ^a   Michel, Hartmut ^b   Ermler, Ulrich ^b  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

^b MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

Author keywords

halophilic enzymes; hyperthermophilic enzymes; methanogenic Archaea; Protein crystallization; X ray crystallography

Indexed keywords

BACTERIAL ENZYME;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ANALYSIS; METHANOBACTERIUM; NONHUMAN; PRIORITY JOURNAL; X RAY DIFFRACTION;

ARCHAEA; CRYSTALLIZATION; CRYSTALLOGRAPHY; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; HYDROXYMETHYL AND FORMYL TRANSFERASES; TEMPERATURE; TRANSFERASES;

EID: 0029797465     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199609)26:1<118::AID-PROT12>3.0.CO;2-J     Document Type: Article

References (27)

1. Donnelly, M.I., Wolfe, R.S. The role of formylmethanofuran:tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide. J. Biol. Chem. 261: 16653-16659, 1986.
2. Wolfe, R.S. My kind of biology. Annu. Rev. Microbiol. 45: 1-35, 1991.
3. 2. In: "Methanogenesis." Ferry, J.G. (eds.). New York: Chapman & Hall, 1993:209-252.
4. 2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus. Arch. Microbiol. 163:112-118, 1995.
5. Huber, R., Kurr, M., Jannasch, H.W., Stetter, K.O. A novel group of abyssal methanogenic archaebacteria (Methanopyrus) growing at 110°C. Nature 342:833-834, 1989.
6. Kurr, M., Huber R., König, H., Jannasch, H.W., Fricke, H., Trincone, Á., Kristjansson, J.K., Stetter, K.O. Methanopyrus kandleri, gen. and sp. nov. represents a novel group of hyperthermophilic methanogens, growing at 110°C. Arch. Microbiol. 156:239-247, 1991.
7. Burggraf, S., Stetter, K.O., Rouvière, P., Woese, C.R. Methanopyrus kandleri: An archaeal methanogen unrelated to all other known methanogens. System. Appl. Microbiol. 14:346-351, 1991.
8. Woese, C.R., Kandler, O., Wheelis, M.L. Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl. Acad. Sci. U.S.A. 87: 4576-4579, 1990.
9. Breitung, J., Börner, G., Scholz, S., Linder, D., Stetter, K.O., Thauer, R.K. Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri. Eur. J. Biochem. 210: 971-981, 1992.
10. Shima, S., Weiss, D.S., Thauer R.K. Formylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr) from the hyperthermophilic Methanopyrus kandleri. Cloning, sequencing and functional expression of the ftr gene and one-step purification of the enzyme overproduced in Escherichia coli. Eur. J. Biochem. 230:906-913, 1995.
11. Menéndez-Arias, L., Argos P. Engineering protein thermal stability. Sequence statistics point to residue substitutions in α-helices. J. Mol. Biol. 206:397-406, 1989.
12. Zwickl, P., Fabry, S., Bogedain, C., Haas, A., Hensel, R. Glyceraldehyde-3-phospate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: Characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli. J. Bacteriol. 172:4329-4338, 1990.
13. Jaenicke, R. Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202:715-728, 1991.
14. Jaenicke, R. Zavodszky, P. Proteins under extreme physical conditions. FEBS Lett. 268:344-349, 1990.
15. Zaccai, G., Eisenberg, H. Halophilic proteins and the influence of solvent on protein stabilization. Trends Biochem. Sci. 15:333-337, 1990.
16. Chan, M.K., Mukund, S., Kletzin, A., Adams, M.W.W., Rees, D.C. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267: 1463-1469, 1995.
17. Yip, K.S.P., Stillman, T.J., Britton, K.L., Artymiuk, P.J., Baker, P.J., Sedelnikova, S.E., Engel, P.C., Pasquo, A., Chiaraluce, R., Consalvi, V., Scandurra, R., Rice, D.W. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 3:1147-1158, 1995.
18. Korndörfer, I., Steipe, B., Huber, R., Tomschy, A., Jaenicke, R. The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 A resolution. J. Mol. Biol. 246:511-521, 1995.
19. Hennig, M., Darimont, B., Sterner, R., Kirschner, K., Jansonius J.N. 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability. Structure 3:1295-1306, 1995.
20. Dym, O., Mevarech, M., Sussman, J.L. Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium. Science 267:1344-1346, 1995.
21. Weiss, D.S., Thauer, R.K. Methanogenesis and the unity of biochemistry. Cell 72:819-822, 1993.
22. Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254, 1976.
23. Jancarik, J., Kim, S.-H. Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24:409-411, 1991.
24. Kabsch, W. Automatic indexing of rotation diffraction patterns. J. Appl. Crystallogr. 21:67-71, 1988.
25. Matthews, B.W. Solvent content of protein crystals. J. Mol. Biol. 33:491-497, 1968.
26. Leslie, A.G.W. Recent changes to the MOSFLM package for processing film and image plate data. In: "Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography, No. 26." Warrington, UK: Daresbury Laboratory, 1992.
27. Collaborative Computational Project, Number 4. The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr. D50:760-763, 1994.