Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium

Structure

Volumn 6, Issue 3, 1998, Pages 351-361

  Russell, Rupert J M ^a   Gerike, Ursula ^a   Danson, Michael J ^a   Hough, David W ^a   Taylor, Garry L ^a  

^a University of Bath   (United Kingdom)

Author keywords

Citrate synthase; Cold denaturation; Cold active; Thermostability

Indexed keywords

BACTERIA (MICROORGANISMS); PYROCOCCUS;

EID: 0032521220     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0969-2126(98)00037-9     Document Type: Article

References (49)

1. Herbert, R.A. (1992). A perspective on the biotechnological potential of extremophiles. Trends Biotechnol. 10, 395-402.
2. Goldman, A. (1995). How to make my blood boil. Structure 3, 1277-1279.
3. Davail, S., Feller, G., Narinx, E. & Gerday, C. (1994). Cold adaptation of proteins. J. Biol. Chem. 269, 17448-17453.
4. Feller, G., Lonhienne, T., Deroanne, C., Libioulle, C., Van Beeumen, J. & Gerday, C. (1992). Purification, characterisation and nucleotide sequence of the thermolabile α-amylase from the Antarctic psychrotroph Alteromonas haloplanctis. J. Biol. Chem. 267, 5217-5221.
5. Rentier-Delrue, F., et al., & Martial, J. (1993). Cloning and overexpression of the triose phosphate isomerase gene from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequence. J. Mol. Biol. 229, 85-93.
6. Wallon, G., et al., Petsko, G.A. (1997). Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp I5 suggest reasons for thermal instability. Protein Eng. 10, 665-672.
7. Tanner, J.J., Hecht, R.M. & Krause, K.L. (1996). Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5 A resolution. Biochemistry 35, 2597-2609.
8. Smalas, A.O., Heimstad, E.S., Hordvik, A., Willasen, P. & Male, R. (1994). Cold adaptation of enzymes: structural comparison between salmon and bovine trypsins. Proteins 20, 149-166.
9. Feller, G., et al., & Gerday, C. (1996). Enzymes from psychrophilic organisms. FEMS Microbiol. Rev. 18, 189-202.
10. Remington, S.J., Wiegand, G. & Huber, R. (1982). Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 Å resolution. J. Mol. Biol. 158, 111-152.
11. Liao, D., Karpusas, M. & Remington, S.J. (1991). Crystal structure of an open conformation of citrate synthase from chicken heart at 2.8 Å resolution. Biochemistry 30, 6031-6036.
12. Russell, R.J.M., Hough, D.W., Danson, M.J. & Taylor, G.L. (1994). The crystal structure of citrate synthase from the thermophilic Archaeon, Thermoplasma acidophilum. Structure 2, 1157-1167.
13. Russell, R.J.M., Ferguson, J.M.C., Hough, D.W., Danson, M.J. & Taylor, G.L. (1997). The crystal structure of citrate synthase from the hyperthermophilic Archaeon Pyrococcus furiosus at 1.9 Å resolution. Biochemistry 36, 9983-9994.
14. Gerike, U., Danson, M.J., Russell, N.J. & Hough, D.W. (1997). Sequencing and expression of the gene encoding a cold-active citrate synthase from Antarctic bacterium, strain DS2-3R. Eur. J. Biochem. 248, 49-57.
15. Muir, J.M., Russell, R.J.M., Hough, D.W. & Danson, M.J. (1995). Citrate synthase from the hyperthermophilic Archaeon Pyrococcus furiosus. Protein Eng. 8, 583-592.
16. Sutherland, K.J., Henneke, C.M., Towner, P., Hough, D.W. & Danson, M.J. (1990). Citrate synthase from the thermophilic archaebacterium Thermoplasma acidophilum. Eur. J. Biochem. 194, 839-844.
17. Aittaleb, M., Hubner, R., Lamotte-Brasseur, J. & Gerday, C. (1997). Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from Antarctic fish Notothenia neglecta. Protein Eng. 10, 475-577.
18. Zhou, H-X., Wong, K-Y. & Vijayakumar, M. (1997). Design of fast enzymes by optimising interaction potential in active sites. Proc. Natl. Acad. Sci. USA 94, 12372-12377.
19. Ermler, U., Merckel, M.C., Thauer, R.K. & Shima, S. (1997). Formylmethanofuran:tetramethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability. Structure 5, 635-646.
20. Danson, M.J. & Hough, D.W. (1997). The structural basis of protein halophilicity. Comp. Biochem. Physiol. 117A, 307-312.
21. Helmstad, E.S., Hansen, L.K. & Smalas, A.O. (1995). Comparative molecular-dynamics simulation studies of salmon and bovine trypsins in aqueous solution. Protein Eng. 8, 379-388.
22. Carr, P.A., Erickson, H.P. & Palmer, A.G. (1997). Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin. Structure 5, 949-959.
23. Bonisch, H., Backmann, J., Kath, T., Naumann, D. & Schafer, G. (1996). Adenylate kinase from Sulfolobus acidocaldarius - expression in Escherichia coli and characterization by Fourier-transform infrared-spectroscopy. Arch. Biochem. Biophys. 333, 75-84.
24. Richardson, J.S. & Richardson, D.C. (1988). Amino acid preferences for specific locations at the ends of α helices. Science 240, 1648-1652.
25. Horovitz, A., Matthews, J.M. & Fersht, A.R. (1992). α-Helix stability in proteins: II. Factors that influence stability at an internal position. J. Mol. Biol. 227, 560-568.
26. Yip, K.S.P., et al., & Rice, D.W. (1995). 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.
27. Feller, G., Payan, F., Theys, F., Qian, M., Haser, R. & Gerday, C. (1994). Stability and structural analysis of α-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. Eur. J. Biochem. 222, 441-447.
28. McDonald, I.K. & Thornton, J.M. (1994). Satisfying hydrogen-bonding potential in proteins. J. Mol. Biol. 238, 777-793.
29. Kleywegt, G.J. & Jones, A.T. (1994). Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Cryst. D 50, 178-185.
30. Privalov, P.L. & Gill, S.J. (1988). Stability of protein structure and Hydrophobic interaction. Adv. Protein Chem. 39, 191-234.
31. Makhatadze, G.I. & Privalov, P.L. (1995). Energetics of protein structure. Adv. Protein Chem. 47, 307-417.
32. Graziano, G., Catanzano, F., Riccio, A. & Barone, G. (1997). A reassessment of the molecular origin of cold-denaturation. J. Biochem. 122, 395-401.
33. Garman, E.F. & Mitchell, E.P. (1996). Flash freezing the "magic 50" (crystal screen 1) crystallisation screen conditions: glycerol concentration required for cryoprotection. J. Appl. Cryst. 29, 584-587.
34. Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-325.
35. Navaza, J. (1994). AMoRE - an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
36. Brünger, A.T., Krukowski, A. & Erickson, J. (1990). Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Cryst. A 46, 585-593.
37. Brünger, A.T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R-factor refinement by molecular dynamics. Science 235, 458-460.
38. CCP4: Collaborative Computational Project No. 4. (1994). Acta. Cryst. D 50, 760-763.
39. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst A 47, 110-119.
40. Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta. Cryst. A 47, 392-400.
41. Brünger, AT. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
42. Jiang, J.S. & Brünger, A.T. (1994). Protein hydration observed by X-ray diffraction: solvation properties of penicllopepsion and neuraminidase crystal structures. J. Mol. Biol. 243, 100-115.
43. Luthy, R., Bowie, J.U. & Eisenberg, D. (1992). Assessment of protein models with 3-dimensional profiles. Nature 356, 83-85.
44. Kraulis, P. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of proteins. J. Appl. Cryst. 24, 946-950.
45. Esnouf, R.E. (1997) An extensively modified version of MOLSCRIPT that includes greatly enhanced colouring capabilities. J. Mol. Graph. Modelling 15, 132-136.
46. Merritt, E.A. & Murphy, M. (1994). Raster3D version 2.0. a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
47. Bacon, D.J. & Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph. 6, 219-220.
48. Barton, G.J. (1993). Alscript - a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
49. Nichols, A., Sharp, K.A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.