Zinc binding drives the folding and association of the homo-trimeric λ-carbonic anhydrase from Methanosarcina thermophila

Protein Engineering, Design and Selection

Volumn 17, Issue 3, 2004, Pages 285-291

  Simler, B Robert ^a   Doyle, Brandon L ^b,c   Matthews, C Robert ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b PENNSYLVANIA STATE UNIVERSITY   (United States)

^c ELI LILLY AND COMPANY   (United States)

Author keywords

helix; Carbonic anhydrase; Trimeric protein assembly; Trimeric protein folding; Zinc binding

Indexed keywords

CARBONATE DEHYDRATASE; GAMMA CARBONIC ANHYDRASE; MONOMER; UNCLASSIFIED DRUG; ZINC ION;

ARTICLE; BETA HELIX; CIRCULAR DICHROISM; ENERGY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STABILITY; METAL BINDING; METHANOSARCINA; METHANOSARCINA THERMOPHILA; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; ULTRACENTRIFUGATION;

BINDING SITES; BIOPOLYMERS; CARBONIC ANHYDRASES; CIRCULAR DICHROISM; ENZYME STABILITY; HISTIDINE; METHANOSARCINA; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROPHOTOMETRY, ULTRAVIOLET; THERMODYNAMICS; ULTRACENTRIFUGATION; UREA; ZINC;

ACTINOBACTERIA (CLASS); HOMO; METHANOSARCINA; METHANOSARCINA THERMOPHILA; UNCULTURED ACTINOMYCETE;

EID: 2942667856     PISSN: 17410126     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/gzh027     Document Type: Article

References (25)

1. Alber, B.E. and Ferry, J.G. (1994) Proc. Natl Acad. Sci. USA, 91, 6909-6913.
2. Beaman, T.W., Binder, D.A., Blanchard, J.S. and Roderick, S.L. (1997) Biochemistry, 36, 489-494.
3. Bracey, M.H., Christiansen, J., Tovar, P., Cramer, S.P. and Bartlett, S.G. (1994) Biochemistry, 33, 13126-13131.
4. Christianson, D.W. and Cox, J.D. (1999) Annu. Rev. Biochem., 68, 33-57.
5. Diamond, D.L. and Randall, L.L. (1997) J. Biol. Chem., 272, 28994-28998.
6. DiTusa, C.A., Christensen, T., McCall, K.A., Fierke, C.A. and Toone, E.J. (2001) Biochemistry, 40, 5338-5344.
7. Hewett-Emmett, D. and Tashian, R.E. (1996) Mol. Phylogenet. Evol., 5, 50-77.
8. Ionescu, R.M., Smith, V.F., O'Neill, J.C., Jr and Matthews, C.R. (2000) Biochemistry, 39, 9540-9550.
9. Kamen, D.E., Griko, Y. and Woody, R.W. (2000) Biochemistry, 39, 15932-15943.
10. Kimber, M.S. and Pai, E.F. (2000) EMBO J., 19, 1407-1418.
11. Kisker, C., Schindelin, H., Alber, B.E., Ferry, J.G. and Rees, D.C. (1996) EMBO J., 15, 2323-2330.
12. Liljas, A. and Laurberg, M. (2000) EMBO Rep., 1, 16-7.
13. Lindskog, S. (1997) Pharmacol. Ther., 74, 1-20.
14. Mitsuhashi, S., Mizushima, T., Yamashita, E., Yamamoto, M., Kumasaka, T., Moriyama, H., Ueki, T., Miyachi, S. and Tsukihara, T. (2000) J. Biol. Chem., 275, 5521-5526.
15. Myers, J.K., Pace, C.N. and Scholtz, J.M. (1995) Protein Sci., 4, 2138-2148.
16. Northrop, D.B. and Simpson, F.B. (1998) Arch. Biochem. Biophys., 352, 288-292.
17. Olsen, L.R. and Roderick, S.L. (2001) Biochemistry, 40, 1913-1921.
18. Raetz, C.R. and Roderick, S.L. (1995) Science, 270, 997-1000.
19. Richardson, J.S. and Richardson, D.C. (2002) Proc. Natl Acad. Sci. USA, 99, 2754-2759.
20. Smith, K.S. and Ferry, J.G. (2000) FEMS Microbiol. Rev., 24, 335-366.
21. Smith, K.S., Jakubzick, C., Whittam, T.S. and Ferry, J.G. (1999) Proc. Natl Acad. Sci. USA, 96, 15184-15189.
22. Tripp, B.C., Smith, K. and Ferry, J.G. (2001) J. Biol. Chem., 276, 48615-48618.
23. Tripp, B.C., Tu, C. and Ferry, J.G. (2002) Biochemistry, 41, 669-678.
24. von Heijne, G. (1985) J. Mol. Biol., 184, 99-105.
25. von Heijne, G. (1986) Nucleic Acids Res., 14, 4683-4690.