Structure of the ATP-binding domain of Plasmodium falciparum Hsp90

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 13, 2010, Pages 2738-2744

  Corbett, Kevin D ^a   Berger, James M ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

ATPase; Drug design; GHKL fold; Malaria

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90;

ARTICLE; DRUG BINDING; HUMAN; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN STRUCTURE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANIMALS; ANTIBIOTICS, ANTINEOPLASTIC; BENZOQUINONES; BINDING SITES; HSP90 HEAT-SHOCK PROTEINS; HYDROGEN BONDING; LACTAMS, MACROCYCLIC; MODELS, MOLECULAR; PLASMODIUM FALCIPARUM; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTOZOAN PROTEINS;

PLASMODIUM FALCIPARUM;

EID: 77957935321     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22799     Document Type: Article

References (24)

1. Pearl LH, Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 2006;75:271-294.
2. Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, Prodromou C, Pearl LH. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 2006;440:1013-1017.
3. Shiau AK, Harris SF, Southworth DR, Agard DA. Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 2006;127:329-340.
4. Acharya P, Kumar R, Tatu U. Chaperoning a cellular upheaval in malaria: heat shock proteins in Plasmodium falciparum. Mol Biochem Parasitol 2007;153:85-94.
5. Mahalingam D, Swords R, Carew JS, Nawrocki ST, Bhalla K, Giles FJ. Targeting HSP90 for cancer therapy. Br J Cancer 2009;100:1523-1529.
6. Roe SM, Prodromou C, O'brien R, Ladbury JE, Piper PW, Pearl LH. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 1999;42:260-266.
7. Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 1994;91:8324-8328.
8. Sharp S, Workman P. Inhibitors of the Hsp90 molecular chaperone: current status. Adv Cancer Res 2006;95:323-348.
9. Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 1997;89:239-250.
10. Banumathy G, Singh V, Pavithra SR, Tatu U. Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. J Biol Chem 2003;278:18336-18345.
11. Kumar R, Musiyenko A, Barik S. The heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycin. Malaria J 2003;2:30.
12. Wider D, Peli-Gulli MP, Briand PA, Tatu U, Picard D. The complementation of yeast with human or Plasmodium falciparum Hsp90 confers differential inhibitor sensitivities. Mol Biochem Parasitol 2009;164:147-152.
13. Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT. Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone. J Biol Chem 2004;279: 46162-46171.
14. Studier FW. Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 2005;41:207-234.
15. Kapust RB, Waugh DS. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 1999;8:1668-1674.
16. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in the oscillation mode. Methods Enzymol 1997;276:307-326.
17. Storoni LC, Mccoy AJ, Read RJ. Likelihood-enhanced fast rotation functions. Acta Crystallogr D Biol Crystallogr 2004;60: 432-438.
18. Prodromou C, Roe SM, O'brien R, Ladbury JE, Piper PW, Pearl LH. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 1997; 90:65-75.
19. Adams PD, Afonine PV, Bunkoczi G, Chen VB, Davis IW, Echols N, Headd JJ, Hung LW, Kapral GJ, Grosse-Kunstleve RW, McCoy AJ, Moriarty NW, Oeffner R, Read RJ, Richardson DC, Richardson JS, Terwilliger TC, Zwart PH. PHENIX: a comprehensive Pythonbased system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 2010;66:213-221.
20. Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004;60:2126-2132.
21. Delano WL. PyMOL. San Carlos, CA: DeLano Scientific; 2002.
22. Dutta R, Inouye M. GHKL, an emergent ATPase/kinase superfamily. Trends Biochem Sci 2000;25:24-28.
23. Obermann WM, Sondermann H, Russo AA, Pavletich NP, Hartl FU. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J Cell Biol 1998;143:901-910.
24. Pavithra SR, Kumar R, Tatu U. Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum. PLoS Comput Biol 2007;3:1701-1715.