Protein Modeling Combined with Spectroscopic Techniques: An Attractive Quick Alternative to Obtain Structural Information

Physiological Research

Volumn 53, Issue SUPPL. 1, 2004, Pages

  Kubala, M ^a,b   Obsil T ^a,b   Obsilova V ^a,b   Lansky Z ^a,b   Amler, E ^a,b  

^a INSTITUTE OF PHYSIOLOGY   (Czech Republic)

^b CHARLES UNIVERSITY   (Czech Republic)

Author keywords

14 3 3 proteins; Computer modeling; Fluorescence spectroscopy; Molecular dynamics simulations; Na+ K+ ATPase; Point mutations; Time resolved fluorescence spectroscopy

Indexed keywords

AMINO ACID; ARGININE; ASPARTIC ACID; GLUTAMIC ACID; GLUTAMINE; GLYCINE; LYSINE; PHENYLALANINE; PROLINE; PROTEIN 14 3 3; THREONINE;

COMPUTER MODEL; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; FLUORESCENCE SPECTROSCOPY; HYDROGEN BOND; MOLECULAR BIOLOGY; MOLECULAR MODEL; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; SEQUENCE HOMOLOGY; SPECTROSCOPY; STEADY STATE;

14-3-3 PROTEINS; ADENOSINE TRIPHOSPHATE; ALCOHOL OXIDOREDUCTASES; AMINO ACID SEQUENCE; BINDING SITES; COMPUTER SIMULATION; CONSERVED SEQUENCE; DNA-BINDING PROTEINS; MODELS, MOLECULAR; NA(+)-K(+)-EXCHANGING ATPASE; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, FLUORESCENCE; THREONINE;

EID: 2342500001     PISSN: 08628408     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (41)

1. 2+-ATPase: probing nucleotide binding by multidimensional NMR. Biochemistry 41: 1156-1164, 2002.
2. +-ATPase. J Biol Chem 268: 21895-21900, 1993.
3. COLLINS JH, LESZYK J: The "gamma subunit" of Na,K-ATPase: a small, amphiphilic protein with a unique amino acid sequence. Biochemistry 26: 8665-8668, 1987.
4. DUBOIS T, ROMMEL C, HOWELL S, STEINHUSSEN U, SONEJI Y, MORRICE N, MOELLING K, AITKEN A: 14-3-3 is phosphorylated by casein kinase I on residue 233 - Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction. J Biol Chem 272: 28882-28888, 1997.
5. +-ATPase deduced by restraint-based comparative modeling shows only one ATP-binding site. J Mol Model 7: 184-192, 2001.
6. FARLEY RA, TRAN CM, CARILLI CT, HAWKE D, SHIVELY JE: The amino acid sequence of a fluorescein-labeled peptide from the active site of (Na,K)-ATPase. J Biol Chem 259: 9532-9535, 1984.
7. FORBUSH B, KAPLAN JH, HOFFMAN JF: Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the Na, K-ATPase. Biochemistry 17: 3667-3676, 1978.
8. FU H, SUBRAMANIAN RR, MASTERS SC: 14-3-3 proteins: structure, function, and regulation. Annu Rev Pharmacol Toxicol 40: 617-647, 2000.
9. GATTO C, WANG AX, KAPLAN JH: The M4M5 cytoplasmic loop of the Na,K-ATPase, overexpressed in Escherichia coli, binds nucleoside triphosphates with the same selectivity as the intact native protein. J Biol Clin 273: 10578-10585, 1998.
10. HAKANSON KO: The crystallographic structure of Na,K-ATPase N-domain at 2.6 A resolution. J Mol Biol 332: 1175-1182, 2003.
11. HEBERT H, PURHONEN P, VORUM H, THOMSEN K, MAUNSBACH AB: Three-dimensional structure of renal Na,K-ATPase from cryo-electron microscopy of two-dimensional crystals. J Mol Biol 314: 479-494, 2001.
12. HILGE M, SIEGAL G, VUISTER GW, GUNTERT P, GLOOR SM, ABRAHAMS JP: ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase. Nat Struct Biol 10: 468-474, 2003.
13. HIRATSUKA T: 2′ (or 3′)-O-(2, 4, 6-trinitrophenyl)adenosine 5′-triphosphate as a probe for the binding site of heavy meromyosin ATPase. J Biochem (Tokyo) 78: 1135-1147, 1975.
14. HIRATSUKA T: Fluorescence properties of 2′ (or 3′ )-O-(2,4,6-trinitrophenyl) adenosine 5′ triphosphate and its use in the study of binding to heavy meromyosin ATPase. Biochim Biophys Acta 453: 293-297, 1976.
15. HIRATSUKA T: Biological activities and spectroscopic properties of chromophoric and fluorescent analogues of adenine nucleoside and nucleotides, 2′,3′-O-(2,4,6-trinitrocyclohexadienylidene) adenosine derivatives. Biochim Biophys Acta 719: 509-517, 1982.
16. HIRATSUKA T, UCHIDA K: Preparation and properties of 2′ (or 3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate, an analogue of adenosine triphosphate. Biochim Biophys Acta 320: 635-647, 1973.
17. 6-(2,4-dinitrophenyl)-adenosine 5′-triphosphate, an analogue of ATP. J Biochem (Tokyo) 74: 649-659, 1973.
18. 567 for high-affinity binding of ATP, ADP, or MgATP. Biochemistry 41: 1451-1456, 2002.
19. +-ATPase. Ann NY Acad Sci 986: 242-244, 2003.
20. +-ATPase. Biochem Biophys Res Commun 297: 154-159, 2002.
21. 5 loop of Na/K-ATPase. Eur Biophys J 32: 363-369, 2003a.
22. +-ATPase. Biochemistry 42: 6446-6452, 2003b.
23. +-ATPase. Physiol Res 53: 109-113, 2004.
24. +-ATPase. Biochemistry (in press) 2004.
25. +-ATPase is slightly acidic. Biochem Biophys Res Commun 254: 215-221, 1999.
26. LIU D, BIENKOWSKA J, PETOSA C, COLLIER RJ, FU H, LIDDINGTON R: Crystal structure of the zeta-isoform of the 14-3-3 protein. Nature 376: 191-194, 1995.
27. MOCZYDLOWSKI EG, FORTES PAG: Characterization of 2′,3′ -O-(2,4,6-trinitrocyclohexadienylidine)adenosine 5′-triphosphate as a fluorescent probe of the ATP site of sodium and potassium transport adenosine triphosphatase. J Biol Chem 256: 2346-2356, 1981.
28. OBŠIL T, GHIRLANDO R, KLEIN DC, GANGULY S, DYDA F: Crystal structure of the 14-3-35 zeta: serotonin N-acetyltransferase complex: a role for scaffolding in enzyme regulation. Cell 105: 257-267, 2001.
29. 232. J Biol Chem 279: 4531-4540, 2004.
30. +-ATPase revealed Asp-710 in the catalytic site. FEBS Lett 217: 111-116, 1987.
31. 2+-catalyzed oxidative cleavage and molecular modeling. Biochemistry 41: 11740-11749, 2002.
32. SCHEINER-BOBIS G, SCHREIBER S: Glutamic acid 472 and lysine 480 of the sodium pump alpha 1 subunit are essential for activity. Their conservation in pyrophosphatases suggests their involvement in recognition of ATP phosphates. Biochemistry 38: 9198-9208, 1999.
33. 2+-ATPase of the sarcoplasmic reticulum. Biochem J 356: 685-704, 2001.
34. TERAMACHI S, IMAGAWA T, KAYA S, TANIGUCHI K: Replacement of several single amino acid side chains exposed to the inside of the ATP-binding pocket induces different extents of affinity change in the high and low affinity ATP-binding sites of rat Na/K-ATPase. J Biol Chem 277: 37394-37400, 2002.
35. TOYOSHIMA C, NOMURA H: Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418: 605-611, 2002.
36. TOYOSHIMA C, NAKASAKO M, NOMURA H, OGAWA H: Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405: 647-655, 2000.
37. TRAN CM, FARLEY RA: Catalytic activity of an isolated domain of Na,K-ATPase expressed in Escherichia coli. Biophys J 77: 258-266, 1999.
38. TRAN CM, HUSTON EE, FARLEY RA: Photochemical labeling and inhibition of Na,K-ATPase by 2-azido-ATP. Identification of an amino acid located within the ATP binding site. J Biol Chem 269: 6558-6565, 1994a.
39. +-ATPase after photochemical labeling with 8-azido-ATP. Biochemistry 33: 4140-4147, 1994b.
40. TRUONG AB, MASTERS SC, YANG H, FU H: Role of the 14-3-3 C-terminal loop in ligand interaction. Proteins 49: 321-325, 2002.
41. VAN HEMERT MJ, STEENSMA HY, VAN HEUSDEN GP: 14-3-3 proteins: key regulators of cell division, signalling and apoptosis. Bioessays 3: 936-946, 2001.