Crystal structure of chicken riboflavin-binding protein.
Abstract
The crystal structure of chicken egg white riboflavin-binding protein, determined to a resolution of 2.5 A, is the prototype of a family that includes other riboflavin- and folate-binding proteins. An unusual characteristic of these molecules is their high degree of cross-linking by disulfide bridges and, in the case of the avian proteins, the presence of stretches of highly phosphorylated polypeptide chain. The structure of chicken egg white riboflavin-binding protein is characterized by a ligand-binding domain and a phosphorylated motif. The ligand-binding domain has a fold that appears to be strongly conditioned by the presence of the disulfide bridges. The phosphorylated motif, essential for vitamin uptake, is made up of two helices found before and after the flexible phosphorylated region. The riboflavin molecule binds to the protein with the isoalloxazine ring stacked in between the rings of Tyr75 and Trp156. This geometry and the proximity of other tryptophans explain the fluorescent quenching observed when riboflavin binds to the protein.
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- Kozik A. Disulfide bonds in egg-white riboflavin-binding protein. Chemical reduction studies. Eur J Biochem. 1982 Jan;121(2):395–400. [PubMed] [Google Scholar]
- Krishnamurthy K, Surolia N, Adiga PR. Mechanism of foetal wastage following immunoneutralization of riboflavin carrier protein in the pregnant rat: disturbances in flavin coenzyme levels. FEBS Lett. 1984 Dec 3;178(1):87–91. [PubMed] [Google Scholar]
- Lubas B, Soltysik M, Steczko J, Ostrowski W. Proton NMR study of the interaction of riboflavin with the egg-yolk apoprotein. FEBS Lett. 1977 Jul 1;79(1):179–182. [PubMed] [Google Scholar]
- Mac Lachlan I, Nimpf J, Schneider WJ. Avian riboflavin binding protein binds to lipoprotein receptors in association with vitellogenin. J Biol Chem. 1994 Sep 30;269(39):24127–24132. [PubMed] [Google Scholar]
- Blankenhorn G. Riboflavin binding in egg-white flavoprotein: the role of tryptophan and tyrosine. Eur J Biochem. 1978 Jan 2;82(1):155–160. [PubMed] [Google Scholar]
- Matsui K, Sugimoto K, Kasai S. Thermodynamics of association of egg yolk riboflavin binding protein with 8-substituted riboflavins. Comparison with the egg white protein. J Biochem. 1982 Apr;91(4):1357–1362. [PubMed] [Google Scholar]
- Becvar J, Palmer G. The binding of flavin derivatives to the riboflavin-binding protein of egg white. A kinetic and thermodynamic study. J Biol Chem. 1982 May 25;257(10):5607–5617. [PubMed] [Google Scholar]
- Choi JD, McCormick DB. The interaction of flavins with egg white riboflavin-binding protein. Arch Biochem Biophys. 1980 Oct 1;204(1):41–51. [PubMed] [Google Scholar]
- Merrill AH, McCormick DB. Flavin affinity chromatography: general methods for purification of proteins that bind riboflavin. Anal Biochem. 1978 Aug 15;89(1):87–102. [PubMed] [Google Scholar]
- Merrill AH, Jr, Froehlich JA, McCormick DB. Purification of riboflavin-binding proteins from bovine plasma and discovery of a pregnancy-specific riboflavin-binding protein. J Biol Chem. 1979 Oct 10;254(19):9362–9364. [PubMed] [Google Scholar]
- Ghisla S, Massey V. New flavins for old: artificial flavins as active site probes of flavoproteins. Biochem J. 1986 Oct 1;239(1):1–12.[PMC free article] [PubMed] [Google Scholar]
- Miller MS, Bruch RC, White HB., 3rd Carbohydrate compositional effects on tissue distribution of chicken riboflavin-binding protein. Biochim Biophys Acta. 1982 Mar 15;715(1):126–136. [PubMed] [Google Scholar]
- Hamazume Y, Mega T, Ikenaka T. Characterization of hen egg white- and yolk-riboflavin binding proteins and amino acid sequence of egg white-riboflavin binding protein. J Biochem. 1984 Jun;95(6):1633–1644. [PubMed] [Google Scholar]
- Miller MS, Benore-Parsons M, White HB., 3rd Dephosphorylation of chicken riboflavin-binding protein and phosvitin decreases their uptake by oocytes. J Biol Chem. 1982 Jun 25;257(12):6818–6824. [PubMed] [Google Scholar]
- Hamazume Y, Mega T, Ikenaka T. Positions of disulfide bonds in riboflavin-binding protein of hen egg white. J Biochem. 1987 Jan;101(1):217–223. [PubMed] [Google Scholar]
- Holt C, Sawyer L. Primary and predicted secondary structures of the caseins in relation to their biological functions. Protein Eng. 1988 Oct;2(4):251–259. [PubMed] [Google Scholar]
- Muniyappa K, Adiga PR. Occurrence and functional importance of a riboflavin-carrier protein in the pregnant rat. FEBS Lett. 1980 Feb 11;110(2):209–212. [PubMed] [Google Scholar]
- Murty CV, Adiga PR. Pregnancy suppression by active immunization against gestation-specific riboflavin carrier protein. Science. 1982 Apr 9;216(4542):191–193. [PubMed] [Google Scholar]
- Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A. 1991 Mar 1;47(Pt 2):110–119. [PubMed] [Google Scholar]
- Natraj U, Kumar R A, Kadam P. Termination of pregnancy in mice with antiserum to chicken riboflavin-carrier protein. Biol Reprod. 1987 Apr;36(3):677–685. [PubMed] [Google Scholar]
- Nishina Y, Shiga K, Horiike K, Tojo H, Kasai S, Matsui K, Watari H, Yamano T. Resonance Raman spectra of semiquinone forms of flavins bound to riboflavin binding protein. J Biochem. 1980 Aug;88(2):411–416. [PubMed] [Google Scholar]
- Norioka N, Okada T, Hamazume Y, Mega T, Ikenaka T. Comparison of the amino acid sequences of hen plasma-, yolk-, and white-riboflavin binding proteins. J Biochem. 1985 Jan;97(1):19–28. [PubMed] [Google Scholar]
- OSTROWSKI W, SKARZYNSKI B, ZAK Z. Isolation and properties of flavoprotein from the egg yolk. Biochim Biophys Acta. 1962 May 21;59:515–517. [PubMed] [Google Scholar]
- Rao ST, Shaffie F, Yu C, Satyshur KA, Stockman BJ, Markley JL, Sundarlingam M. Structure of the oxidized long-chain flavodoxin from Anabaena 7120 at 2 A resolution. Protein Sci. 1992 Nov;1(11):1413–1427.[PMC free article] [PubMed] [Google Scholar]
- RHODES MB, BENNETT N, FEENEY RE. The flavoprotein-apoprotein system of egg white. J Biol Chem. 1959 Aug;234(8):2054–2060. [PubMed] [Google Scholar]
- Rohrer JS, White HB., 3rd Separation and characterization of the two Asn-linked glycosylation sites of chicken serum riboflavin-binding protein. Glycosylation differences despite similarity of primary structure. Biochem J. 1992 Jul 1;285(Pt 1):275–280.[PMC free article] [PubMed] [Google Scholar]
- Tarutani M, Norioka N, Mega T, Hase S, Ikenaka T. Structures of sugar chains of hen egg yolk riboflavin-binding protein. J Biochem. 1993 Jun;113(6):677–682. [PubMed] [Google Scholar]
- Visweswariah SS, Adiga PR. Purification of a circulatory riboflavin carrier protein from pregnant bonnet monkey (M. radiata): comparison with chicken egg vitamin carrier. Biochim Biophys Acta. 1987 Sep 24;915(2):141–148. [PubMed] [Google Scholar]
- Walsh C, Fisher J, Spencer R, Graham DW, Ashton WT, Brown JE, Brown RD, Rogers EF. Chemical and enzymatic properties of riboflavin analogues. Biochemistry. 1978 May 16;17(10):1942–1951. [PubMed] [Google Scholar]
- Watenpaugh KD, Sieker LC, Jensen LH. The binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin at 2.0-Angstrom resolution. Proc Natl Acad Sci U S A. 1973 Dec;70(12):3857–3860.[PMC free article] [PubMed] [Google Scholar]
- Wessiak A, Schopfer LM, Yuan LC, Bruice TC, Massey V. Use of riboflavin-binding protein to investigate steric and electronic relationships in flavin analogs and models. Proc Natl Acad Sci U S A. 1984 Jul;81(14):4246–4249.[PMC free article] [PubMed] [Google Scholar]
- White HB, 3rd, Merrill AH., Jr Riboflavin-binding proteins. Annu Rev Nutr. 1988;8:279–299. [PubMed] [Google Scholar]
- Zanette D, Monaco HL, Zanotti G, Spadon P. Crystallization of hen eggwhite riboflavin-binding protein. J Mol Biol. 1984 Dec 25;180(4):1185–1187. [PubMed] [Google Scholar]
- Zheng DB, Lim HM, Pène JJ, White HB., 3rd Chicken riboflavin-binding protein. cDNA sequence and homology with milk folate-binding protein. J Biol Chem. 1988 Aug 15;263(23):11126–11129. [PubMed] [Google Scholar]
Abstract
The crystal structure of chicken egg white riboflavin-binding protein, determined to a resolution of 2.5 A, is the prototype of a family that includes other riboflavin- and folate-binding proteins. An unusual characteristic of these molecules is their high degree of cross-linking by disulfide bridges and, in the case of the avian proteins, the presence of stretches of highly phosphorylated polypeptide chain. The structure of chicken egg white riboflavin-binding protein is characterized by a ligand-binding domain and a phosphorylated motif. The ligand-binding domain has a fold that appears to be strongly conditioned by the presence of the disulfide bridges. The phosphorylated motif, essential for vitamin uptake, is made up of two helices found before and after the flexible phosphorylated region. The riboflavin molecule binds to the protein with the isoalloxazine ring stacked in between the rings of Tyr75 and Trp156. This geometry and the proximity of other tryptophans explain the fluorescent quenching observed when riboflavin binds to the protein.