| Literature DB >> 1332027 |
M R Chance1, I Sagi, M D Wirt, S M Frisbie, E Scheuring, E Chen, J W Bess, L E Henderson, L O Arthur, T L South.
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.Entities:
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Year: 1992 PMID： 1332027 PMCID： PMC50273 DOI： 10.1073/pnas.89.21.10041
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205