Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1992 Nov 1;89(21):10041–10045. doi: 10.1073/pnas.89.21.10041

Extended x-ray absorption fine structure studies of a retrovirus: equine infectious anemia virus cysteine arrays are coordinated to zinc.

M R Chance 1, I Sagi 1, M D Wirt 1, S M Frisbie 1, E Scheuring 1, E Chen 1, J W Bess Jr 1, L E Henderson 1, L O Arthur 1, T L South 1, et al.
PMCID: PMC50273  PMID: 1332027

Abstract

Zinc finger arrays have been established as a critical structural feature of proteins involved in DNA recognition. Retroviral nucleocapsid proteins, which are involved in the binding of viral RNA, contain conserved cysteine-rich arrays that have been suggested to coordinate zinc. We provide metalloprotein structural data from an intact virus preparation that validate this hypothesis. Extended x-ray absorption fine structure (EXAFS) spectroscopy of well-characterized and active preparations of equine infectious anemia virus, compared with a peptide with known coordination and in combination with available biochemical and genetic data, defines a Cys3His1 coordination environment for zinc. The average of the Zn-S distances is 2.30(1) A and that of the Zn-N distance (to histidine) is 2.01(3) A.

Full text

PDF
10042

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Berg J. M. Potential metal-binding domains in nucleic acid binding proteins. Science. 1986 Apr 25;232(4749):485–487. doi: 10.1126/science.2421409. [DOI] [PubMed] [Google Scholar]
  2. Bess J. W., Jr, Powell P. J., Issaq H. J., Schumack L. J., Grimes M. K., Henderson L. E., Arthur L. O. Tightly bound zinc in human immunodeficiency virus type 1, human T-cell leukemia virus type I, and other retroviruses. J Virol. 1992 Feb;66(2):840–847. doi: 10.1128/jvi.66.2.840-847.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chance M., Powers L., Kumar C., Chance B. X-ray absorption studies of myoglobin peroxide reveal functional differences between globins and heme enzymes. Biochemistry. 1986 Mar 25;25(6):1259–1265. doi: 10.1021/bi00354a010. [DOI] [PubMed] [Google Scholar]
  4. Copeland T. D., Morgan M. A., Oroszlan S. Complete amino acid sequence of the basic nucleic acid binding protein of feline leukemia virus. Virology. 1984 Feb;133(1):137–145. doi: 10.1016/0042-6822(84)90432-x. [DOI] [PubMed] [Google Scholar]
  5. Diakun G. P., Fairall L., Klug A. EXAFS study of the zinc-binding sites in the protein transcription factor IIIA. Nature. 1986 Dec 18;324(6098):698–699. doi: 10.1038/324698a0. [DOI] [PubMed] [Google Scholar]
  6. Freedman L. P., Luisi B. F., Korszun Z. R., Basavappa R., Sigler P. B., Yamamoto K. R. The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain. Nature. 1988 Aug 11;334(6182):543–546. doi: 10.1038/334543a0. [DOI] [PubMed] [Google Scholar]
  7. Gorelick R. J., Henderson L. E., Hanser J. P., Rein A. Point mutants of Moloney murine leukemia virus that fail to package viral RNA: evidence for specific RNA recognition by a "zinc finger-like" protein sequence. Proc Natl Acad Sci U S A. 1988 Nov;85(22):8420–8424. doi: 10.1073/pnas.85.22.8420. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gorelick R. J., Nigida S. M., Jr, Bess J. W., Jr, Arthur L. O., Henderson L. E., Rein A. Noninfectious human immunodeficiency virus type 1 mutants deficient in genomic RNA. J Virol. 1990 Jul;64(7):3207–3211. doi: 10.1128/jvi.64.7.3207-3211.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Green L. M., Berg J. M. A retroviral Cys-Xaa2-Cys-Xaa4-His-Xaa4-Cys peptide binds metal ions: spectroscopic studies and a proposed three-dimensional structure. Proc Natl Acad Sci U S A. 1989 Jun;86(11):4047–4051. doi: 10.1073/pnas.86.11.4047. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Green L. M., Berg J. M. Retroviral nucleocapsid protein-metal ion interactions: folding and sequence variants. Proc Natl Acad Sci U S A. 1990 Aug;87(16):6403–6407. doi: 10.1073/pnas.87.16.6403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Henderson L. E., Copeland T. D., Sowder R. C., Smythers G. W., Oroszlan S. Primary structure of the low molecular weight nucleic acid-binding proteins of murine leukemia viruses. J Biol Chem. 1981 Aug 25;256(16):8400–8406. [PubMed] [Google Scholar]
  12. Jentoft J. E., Smith L. M., Fu X. D., Johnson M., Leis J. Conserved cysteine and histidine residues of the avian myeloblastosis virus nucleocapsid protein are essential for viral replication but are not "zinc-binding fingers". Proc Natl Acad Sci U S A. 1988 Oct;85(19):7094–7098. doi: 10.1073/pnas.85.19.7094. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Méric C., Goff S. P. Characterization of Moloney murine leukemia virus mutants with single-amino-acid substitutions in the Cys-His box of the nucleocapsid protein. J Virol. 1989 Apr;63(4):1558–1568. doi: 10.1128/jvi.63.4.1558-1568.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Peisach J., Powers L., Blumberg W. E., Chance B. Stellacyanin. Studies of the metal-binding site using x-ray absorption spectroscopy. Biophys J. 1982 Jun;38(3):277–285. doi: 10.1016/S0006-3495(82)84559-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Powers L., Chance B., Ching Y., Angiolillo P. Structural features and the reaction mechanism of cytochrome oxidase: iron and copper X-ray absorption fine structure. Biophys J. 1981 Jun;34(3):465–498. doi: 10.1016/S0006-3495(81)84863-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Roberts W. J., Pan T., Elliott J. I., Coleman J. E., Williams K. R. p10 single-stranded nucleic acid binding protein from murine leukemia virus binds metal ions via the peptide sequence Cys26-X2-Cys29-X4-His34-X4-Cys39. Biochemistry. 1989 Dec 26;28(26):10043–10047. doi: 10.1021/bi00452a024. [DOI] [PubMed] [Google Scholar]
  17. South T. L., Blake P. R., Hare D. R., Summers M. F. C-terminal retroviral-type zinc finger domain from the HIV-1 nucleocapsid protein is structurally similar to the N-terminal zinc finger domain. Biochemistry. 1991 Jun 25;30(25):6342–6349. doi: 10.1021/bi00239a036. [DOI] [PubMed] [Google Scholar]
  18. Summers M. F., Henderson L. E., Chance M. R., Bess J. W., Jr, South T. L., Blake P. R., Sagi I., Perez-Alvarado G., Sowder R. C., 3rd, Hare D. R. Nucleocapsid zinc fingers detected in retroviruses: EXAFS studies of intact viruses and the solution-state structure of the nucleocapsid protein from HIV-1. Protein Sci. 1992 May;1(5):563–574. doi: 10.1002/pro.5560010502. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Summers M. F., South T. L., Kim B., Hare D. R. High-resolution structure of an HIV zinc fingerlike domain via a new NMR-based distance geometry approach. Biochemistry. 1990 Jan 16;29(2):329–340. doi: 10.1021/bi00454a005. [DOI] [PubMed] [Google Scholar]
  20. Tajima M., Nakajima H., Ito Y. Electron microscopy of equine infectious anemia virus. J Virol. 1969 Oct;4(4):521–527. doi: 10.1128/jvi.4.4.521-527.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES