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.

引用

页码：10041 / 10045

页数：5

共 31 条

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