EXTENDED X-RAY ABSORPTION FINE-STRUCTURE STUDIES OF A RETROVIRUS - EQUINE INFECTIOUS-ANEMIA VIRUS CYSTEINE ARRAYS ARE COORDINATED TO ZINC

被引：53
作者：
CHANCE, MR
SAGI, I
WIRT, MD
FRISBIE, SM
SCHEURING, E
CHEN, E
BESS, JW
HENDERSON, LE
ARTHUR, LO
SOUTH, TL
PEREZALVARADO, G
SUMMERS, MF
机构：
[1] GEORGETOWN UNIV, DEPT CHEM, WASHINGTON, DC 20057 USA
[2] NCI, FREDERICK CANC RES & DEV CTR, PROGRAM RESOURCES INC DYN CORP, FREDERICK, MD 21701 USA
[3] UNIV MARYLAND, DEPT CHEM & BIOCHEM, CATONSVILLE, MD 21228 USA
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1992年 / 89卷 / 21期
关键词：
D O I：
10.1073/pnas.89.21.10041
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
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) angstrom and that of the Zn-N distance (to histidine) is 2.01(3) angstrom.
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页码：10041 / 10045
页数：5
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