EF-hands at atomic resolution: The structure of human psoriasin (S100A7) solved by MAD phasing

Structure

Volumn 6, Issue 4, 1998, Pages 477-489

  Brodersen, D E ^a   Etzerodt, M ^a   Madsen, P ^a   Celis, J E ^a   Thogersen H C ^a   Nyborg, J ^a   Kjeldgaard, M ^a  

^a AARHUS UNIVERSITY   (Denmark)

Author keywords

EF hand protein; MAD phasing; Psoriasis; S100 protein family; X ray crystallography

Indexed keywords

EID: 0032522812     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00049-5     Document Type: Article

References (42)

1. Moore, B.A. (1965). A soluble protein characteristic of the nervous system. Biochem. Biophys. Res. Commun. 19, 739-744.
2. Schäfer, B.W. & Heizmann, C.W. (1996). The S100 family of EF-hand calcium-binding proteins: functions and pathology. Trends Biochem. Sci. 21, 134-140.
3. Tufty, R.M. & Kretsinger, R.H. (1975). Troponin and parvalbumin calcium-binding regions predicted in myosin light chain and T4 Iysozyme. Science 187, 167-169.
4. Hoffmann, H.J., et al., & Celis, J.E. (1994). Psoriasin binds calcium and is up-regulated by calcium to levels that resemble those observed in normal skin. J. Invest. Dermatol. 103, 370-375.
5. Kilby, P.M., Eldik, L.J.V. & Roberts, G.C.K. (1996). The solution structure of the bovine S100B protein dimer in the calcium-free state. Structure 4, 1041-1052.
6. 2+-binding proteins. Nat. Struct. Biol. 2, 790-796.
7. 2+. J. Mol. Biol. 236, 953-957.
8. Szebenyi, D.E. & Moffat, K. (1986). The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. J. Biol. Chem. 261, 8761-8777.
9. 9k determined by nuclear magnetic resonance spectroscopy. Biochemistry 31, 1011-1020.
10. 9k by NMR spectroscopy. J. Mol. Biol. 249, 441-462.
11. Weis, W.I., Kahn, R., Fourme, R., Drickamer, K. & Hendrickson, W. (1991). Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing. Science 254, 1608-1615.
12. Burling, F.T., Weis, W.I., Flaherty, K.M. & Brünger, A.T. (1996). Direct observation of protein solvation and discrete disorder with experimental crystallographic phases. Science 271, 72-77.
13. Flaherty, K.M., Zozulya, S., Stryer, L. & McKay, D.B. (1993). Three-dimensional structure of recoverin, a calcium sensor in vision. Cell 75, 709-716.
14. Nolsøe, S., Thirup, S., Etzerodt, M., Thøgersen, H.C. & Nyborg, J. (1997). Crystallization and preliminary X-ray diffraction studies of psoriasin. Acta Cryst. D 53, 119-121.
15. CCP4. (1994). The CCP4 Suite: programs for proteins crystallography. Acta Cryst. D 50, 760-763.
16. Hendrickson, W. (1991). Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58.
17. de La Fortelle, E. & Bricogne, G. (1997). SHARP: a maximum-likelihood heavy-atom parameter refinement program for the MIR and MAD methods. In Methods in Enzymology. (Carter, C.W. & Sweet, R.M., eds), pp. 472-494, 276, Academic Press, USA.
18. Ramakrishnan, V. & Biou, V. (1997). Treatment of MAD data as a special case of MIR. In Methods in Enzymology. (Carter, C.W. & Sweet, R.M., eds), pp. 538-557, 276, Academic Press, USA.
19. Tronrud, D.E. (1992). Conjugate-direction minimization: an improved method for the refinement of macromolecules. Acta Cryst. A 48, 912-916.
20. Sheldrick, G.M. (1993). SHELX-93: A program for crystal structure refinement. University of Göttingen, Göttingen, Germany.
21. Sheldrick, G.M. & Schneider, T.R. (1997). SHELXL: high-resolution refinement. In Methods in Enzymology. (Carter, C.W. & Sweet, R.M., eds), pp. 319-343, 276, Academic Press, USA.
22. Read, R. (1986). Improved fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A 42, 140-149.
23. Lin, G., et al., & Narayana, S.V. (1997). Crystal structure of calcium bound domain VI of calpain at 1.9Å resolution and its role in enzyme assembly, regulation, and inhibitor binding. Nat. Struct. Biol. 4, 539-547.
24. Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: graphical representation and analysis of surface properties. Biophys. J. 64, 166-170.
25. Wright, N.A. & Camplejohn, R.S. (1985). Psoriasis: Cell Proliferation. (Camplejohn, R.S., ed), Churchhill Livingstone, Edinburgh.
26. Celis, J.E., et al., & Bauw, G. (1990). A two-dimensional gel protein database of noncultured total normal human epidermal keratinocytes: identification of proteins strongly up- regulated in psoriatic epidermis. Electrophoresis 11, 242-254.
27. Celis, J.E., et al., Celis, A. (1990). Identification of a group of proteins that are strongly up-regulated in total epidermal keratinocytes from psoriatic skin. FEBS letts. 262, 159-164.
28. Madsen, P., Rasmussen, H.H., Letters, H., Honoré, B. & Celis, J.E. (1992). Molecular cloning and expression of a novel keratinocyte protein (psoriasis-associated fatty acid-binding protein [PA-FABP]) that is highly up-regulated in psoriatic skin and that shares similarity to fatty acid-binding proteins. J. Invest. Dermatol. 99, 299-305.
29. Madsen, P., et al., & Celis, J.E. (1991). Molecular cloning, occurrence, and expression of a novel partially secreted protein "psoriasin" that is highly up-regulated in psoriatic skin. J. Invest. Dermatol. 97, 701-712.
30. Rasmussen, H.H. & Celis, J.E. (1993). Evidence for an altered protein kinase C (PKC) signaling pathway in psoriasis. J. Invest. Dermatol. 101, 560-566.
31. Porath, J. (1992). Immobilized metal ion affinity chromatography. Protein Expr. Pur. 3, 263-281.
32. Otwinowski, Z. (1993). Oscillation and data reduction program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp. 56-62, Daresbury Laboratory, Warrington, UK.
33. Jones, T.A., Cowan, S., Zou, J.-Y. & 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.
34. Brünger, A. (1992). Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
35. Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
36. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
37. Luzzati, V. (1952). Traitement statistique des erreurs dans la determination des structures cristallines. Acta Cryst. 5, 802-810.
38. Kleywegt, G.J. & Jones, T.A. (1996). Phi/psi-chology: Ramachandran revisited. Structure 4, 1395-1400.
39. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
40. Bacon, D.J. & Anderson, W.F. (1988). A fast algoritm for rendering space-filled molecule pictures. J. Mol. Graphics 6, 219-220.
41. Merritt, E.A. & Murphy, M.E.P. (1994). Raster3D Version 2.0: a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
42. Corpet, F. (1988). Multiple sequence alignment with hierarchical clustering. Nucl. Acids Res. 16, 10881-10890.