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

Identifieur interne : 004652 ( Main/Exploration ); précédent : 004651; suivant : 004653

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

Auteurs : M. Milani [Italie] ; L. Andolfi ; S. Cannistraro ; M P Verbeet ; M. Bolognesi

Source :

RBID : pubmed:11679761

Descripteurs français

English descriptors

Abstract

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 A 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.

DOI: 10.1107/s0907444901013221
PubMed: 11679761


Affiliations:


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Le document en format XML

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