Extended x-ray absorption fine structure studies of a retrovirus: equine infectious anemia virus cysteine arrays are coordinated to zinc.
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.
Chance
M R
MR
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461.
Sagi
I
I
Wirt
M D
MD
Frisbie
S M
SM
Scheuring
E
E
Chen
E
E
Bess
J W
JW
Henderson
L E
LE
Arthur
L O
LO
South
T L
TL
D015502:Absorptiometry, Photon / Q000379:methods; D002499:Centrifugation, Density Gradient; D003545:Cysteine; D005583:Fourier Analysis; D015497:HIV-1 / Q000648:ultrastructure; D004860:Infectious Anemia Virus, Equine / Q000648:ultrastructure*; D014764:Viral Proteins / Q000648:ultrastructure*; D015032:Zinc / Q000032:analysis*; D016335:Zinc Fingers
D014764:Viral Proteins; D015032:Zinc; D003545:Cysteine