High-resolution structures of retinol-binding protein in complex with retinol: pH-induced protein structural changes in the crystal state

Journal of Molecular Biology

Volumn 329, Issue 4, 2003, Pages 841-850

  Calderone, Vito ^a,d   Berni, Rodolfo ^b   Zanotti, Giuseppe ^a,c  

^a UNIVERSITY OF PADOVA   (Italy)

^b UNIVERSITY OF PARMA   (Italy)

^c VENETIAN INSTITUTE OF MOLECULAR MEDICINE   (Italy)

^d UNIVERSITY OF SIENA   (Italy)

Author keywords

Crystal structure; RBP; Retinoids; Retinol binding protein; Vitamin A

Indexed keywords

CARRIER PROTEIN; HYDROGEN; LIGAND; RETINOL BINDING PROTEIN; SOLVENT;

ACIDITY; ALKALINITY; ARTICLE; CHEMICAL BOND; CRYSTAL STRUCTURE; DENATURATION; EVIDENCE BASED MEDICINE; MOLECULE; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN STRUCTURE;

BOVINAE;

EID: 0038730769     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00468-6     Document Type: Article

References (27)

1. Newcomer M.E., Jones T.A., Aqvist J., Sundelin J., Eriksson U., Rask L., Peterson P.A. The three-dimensional structure of retinol-binding protein. EMBO J. 3:1984;1451-1454.
2. Cowan S.W., Newcomer M.E., Jones T.A. Crystallographic refinement of human serum retinol binding protein at 2 Å resolution. Proteins: Struct. Funct.Genet. 8:1990;44-61.
3. Zanotti G., Berni R., Monaco H.L. Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding protein. J. Biol. Chem. 268:1993;10728-10738.
4. Zanotti G., Panzalorto M., Marcato A., Malpeli G., Folli C., Berni R. Structure of pig plasma retinol-binding protein at 1.65 Å resolution. Acta Crystallog. D54:1998;1049-1052.
5. Zanotti G., Calderone V., Beda M., Malpeli G., Folli C., Berni R. Structure of chicken plasma retinol-binding protein. Biochim. Biophys. Acta. 1550:2001;64-69.
6. Zanotti G., Ottonello S., Berni R., Monaco H.L. Crystal structure of the trigonal form of human plasma retinol-binding protein at 2.5 Å resolution. J. Mol. Biol. 230:1993;613-624.
7. Bychkova V.E., Berni R., Rossi G.L., Kutyshenko P., Ptitsyn O.B. Retinol-binding protein is in the molten globule state at low pH. Biochemistry. 31:1992;7566-7571.
8. Ptitsyn O.B., Zanotti G., Denesyuk A.N., Bychkova V.E. Mechanism of pH-induced release of retinol from retinol-binding protein. FEBS Letters. 317:1993;181-184.
9. Bychkova V.E., Dujsekina A.E., Fantuzzi A., Ptitsyn O.B., Rossi G.L. Release of retinol and denaturation of its plasma carrier, retinol-binding protein. Fold. Des. 3:1998;285-291.
10. Monaco H.L., Rizzi M., Coda A. Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein. Science. 268:1995;1039-1041.
11. Naylor H.M., Newcomer M.E. The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP. Biochemistry. 38:1999;2647-2653.
12. 2. Acta Crystallog. B28:1972;2936-2945.
13. Hamanaka T., Mitsui T., Ashida T., Kakudo M. The crystal structure of all-trans retinal. Acta Crystallog. B28:1972;214-222.
14. Cowan S.W., Newcomer M.E., Jones T.A. Crystallographic studies on a family of cellular lipophilic transport proteins. Refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans-retinol. J. Mol. Biol. 230:1993;1225-1246.
15. Winter N.S., Bratt J.M., Banaszak L.J. Crystal structures of holo and apo-cellular retinol-binding protein II. J. Mol. Biol. 230:1993;1247-1259.
16. Calderone V., Folli C., Marchesani A., Berni R., Zanotti G. Identification and structural analysis of a zebrafish apo and holo cellular retinol-binding protein. J. Mol. Biol. 321:2002;527-535.
17. Takano K., Tsuchimori K., Yamagata Y., Yutani K. Contribution of salt bridges near the surface of a protein to the conformational stability. Biochemistry. 39:2000;12375-12381.
18. Kumar S., Nussinov R. Relationship between ion pair geometries and electrostatic strengths in proteins. Biophys. J. 83:2002;1595-1612.
19. Dong F., Zhou H.X. Electrostatic contributions to T4 lysozyme stability: Solvent-exposed charges versus semi-buried salt bridges. Biophys. J. 83:2002;1341-1347.
20. Loladze V.V., Makhatadze G.I. Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable. Protein Sci. 11:2002;174-177.
21. Berni R., Lamberti V. Dissociation of the bovine serum retinol-binding protein-transthyretin complex and purification of the two interacting proteins. Comp. Biochem. Physiol. 94B:1989;79-83.
22. Leslie A.G.W. Crystallographic Computing. 1990;Oxford University Press, Oxford.
23. The CCP4 Suite: programs for protein crystallography. Acta Crystallog. D50:1994;760-763.
24. Sheldrick G.M., Schneider T.R. SHELXL: high resolution refinement. Sweet R.M., Carter C.W. Jr. Methods in Enzymology. Vol. 277:1997;319-343 Academic Press, Orlando, Florida.
25. McRee D.E. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125:1999;156-165.
26. Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. Procheck. A program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 25:1993;283-291.
27. Kleywegt G.J., Jones T.A. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallog. D50:1994;178-185.