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. 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.

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Selected References

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

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