The 1.6 Å resolution crystal structure of a mutant plastocyanin bearing a 21-25 engineered disulfide bridge

被引：11

作者：

Milani, M

Andolfi, L

Cannistraro, S

Verbeet, MP

Bolognesi, M

机构：

[1] Univ Genoa, Adv Biotechnol Ctr IST, INFM, Dept Phys, I-16132 Genoa, Italy

[2] Ist Giannina Gaslini, I-16147 Genoa, Italy

[3] Univ Tuscia, Dipartimento Sci Ambientali, Unita INFM, I-01100 Viterbo, Italy

[4] Leiden Univ, Gorlaeus Labs, Leiden Inst Chem, NL-2300 RA Leiden, Netherlands

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444901013221

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Plastocyanin is an electron-transfer protein which has been largely used for biophysical studies as well as for protein-engineering experiments. A surface disulfide bridge has been engineered in poplar plastocyanin to allow protein chemisorption on gold substrates. The mutated plastocyanin crystal structure has been studied at 1.6 Angstrom resolution (R factor = 0.145, R-free = 0.205) to characterize the effects of the engineered disulfide on the overall protein structure and on the Cu-coordination sphere in view of biophysical applications. The new orthorhombic crystal form isolated for the mutated plastocyanin displays two protein molecules per asymmetric unit.

引用

页码：1735 / 1738

页数：4