The π-helix translates structure into function

Protein Science

Volumn 9, Issue 1, 2000, Pages 201-206

  Weaver, Todd M ^a  

^a UNIVERSITY OF WISCONSIN LA CROSSE   (United States)

Author keywords

Catechol o methyltransferase; Fumarase C; Glycogen phosphorylase; Lipoxygenase; Photoactive yellow protein; Secondary structure; Serine carboxypeptidase; helix; helix

Indexed keywords

CATECHOL METHYLTRANSFERASE; FUMARATE HYDRATASE; GLYCOGEN PHOSPHORYLASE; LIPOXYGENASE; SERINE CARBOXYPEPTIDASE;

ARTICLE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION;

EID: 0033978466     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.1.201     Document Type: Article

References (32)

1. Barlow DJ, Thornton JM. 1988. Helix geometry in proteins. J Mol Biol 201:601-619.
2. Bash PA, Pattabiraman N, Huang CC, Ferrin TE, Langridge R. 1983. Van der Waal's surfaces in molecular modeling: Implementation with real-time computer graphics. Science 222:1325-1327.
3. Borstahl GE, Williams DR, Getzoff ED 1995. 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site and chromophore. Biochemistry 34:6278-6287.
4. Boyington JC, Gaffney BJ, Amzel LM. 1993. The three-dimensional structure of an arachidonic acid 15-lipoxygenase. Science 260:1482-1486.
5. Donohue J. 1953. Hydrogen bonded helical configurations of the polypeptide chain. Proc Natl Acad Sci USA 39:470-478.
6. Dunharn WR, Carroll RT, Thompson JE, Sands RH, Funk MO Jr. 1990. The initial characterization of the iron environment in lipoxygenase by Mosshauer spectroscopy. Eur J Biochem 190:611-617.
7. Ely KR, Herron JN, Harker M, Edmundson AB. 1989. Three-dimensional structure of a light-chain dimer crystallised in water. J Mol Biol 210:601-615.
8. Ferrin TE, Huang CC, Jarvis LE, Langridge R. 1988. The Midas display system. J Mol Graphics 6:13-30.
9. Fletterick RJ, Madsen NB. 1980. The structures and related functions of phosphorylase a. In: Snell EE, Buyer PD, Meister A, Richardson CC. eds. Annual review biochemistry. Palo Alto, CA: Annual Reviews Inc. pp 31-61.
10. Gaffney BJ. 1996. Lipoxygenases: Structural principles and spectroscopy. Ann Rev Biophys Biomol Struct 25:431-459.
11. Graves DJ, Wang JH. 1972. α-Glucan phosphorylases - Chemical and physical basis of catalysis and regulation. In: Boyer PD, ed. The enzymes. London: Academic Press. pp 435-482.
12. Huang CC, Pettersen EF, Klein TE, Ferrin TE, Langridge R. 1991. Conic: A fast renderer for space-filling molecules with shadows. J Mol Graphics 9:230-236.
13. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A47:110-119.
14. Kabsch W, Sander C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637
15. Klein HW, Palm D, Helmrich JM. 1982. General acid-base catalysis of alphaglucan phosphorylase: Stereospecific glucosyl transfer from D-glucal is a pyridoxal 5′-phosphate and orthophosphate (arsenate) dependent reaction. Biochemistry 21:6675-6684.
16. Laskowski RA, Mac-Arthur MW, Moss DS, Thornton JM. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Ciystallogr 26:283-291.
17. Liao D, Breddam K, Sweet R, Bullock T, Remington SJ. 1992. Refined atomic-model of wheat serine carboxypeptiduse II at 2,2 A resolution. Biochemistry 31:9796-9812.
18. Low BW, Baybutt RB. 1952. The π-helix - A hydrogen bonded configuration of the polypeptide chain. J Am Chem Soc 74:5806.
19. Low BW, Greenville-Wells HJ. 1953. Generalized mathematical relationships for polypeptide chain helices. The coordinates of the π-helix. Proc Natl Acad Sci USA 39:785-801.
20. Minor W, Steczko J, Bolin JT, Olwinowski Z, Axelrod B. 1993. Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1. Biochemistry 32:6320-6323.
21. Pauling L, Corey RB. 1951. Atomic coordinates and structure factors for two helical configurations of polypeptide chains. Proc Ntal Acad Sci USA 37:235-240.
22. Peters JW, Stowell MHB, Soltis SM, Finnegan MG, Johnson MK, Rees DC, 1997. Redox-dependent structural changes in the nitrogenase P-cluster. Biochemistry 36:1181-1187.
23. Ramanchandran G, Sasisekharan V. 1968. Conformation of polypeptides and proteins. Adv Prot Chem 25:284-438.
24. 10-helix/coli transitions isolated in peptides. Protein Sci 5:1687-1696.
25. Rohl CA, Scholtz JM, York EJ, Stewart JM, Baldwin RL. 1992. Kinetics of amide proton exchange in helical peptides of varying lengths: Interpretation by Lifson-Roig equation. Biochemistry 31:1263-1269.
26. Shoichet BK, Baase WA, Kuroki R, Matthews BW. 1995. A relationship between protein stability and protein function. Proc Natl Acad Sci 92:452-456.
27. Steczko J, Donoho GP, Clemens JC, Dixon JE, Axelrod B. 1992. Conserved histidine residues in soybean lipoxygenase: Functional consequences of their replacement. Biochemistry 31:4053-4057.
28. Vldgren J, Svensson LA, Lijjas A. 1994. Crystal structure of catechol-O-methyltransferase. Nature 368:354.
29. Weaver TM, Banaszak LJ. 1996. Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Biochemistry 35:13955-13965.
30. Weaver TM, Lees M, Zaitsev V, Zaitseva I, Duke E, Lindley P, McSweeny S, Svensson A, Keruchenko J, Keruchenko I, et al. 1998. Crystal structures of native and recombinant yeast fumarase. J Mol Biol 280:431-442.
31. Weaver TM, Levitt DG, Donnelly MI, Barnes-Wilkens PP, Banaszak LJ. 1995. The multi-subunit active site of fumarase C from Escherichia coli. Nat Struct Biol 2:654-662.
32. Withers JH, Madsen NB, Sprang SR, Fletterick RJ. 1982. Catalytic site of glycogen phosphorylase: structural changes during activation and mechanistic implications. Biochemistry 27:5372-5382.