1aqe

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[[Category: point mutant]]
[[Category: point mutant]]
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Revision as of 12:46, 30 October 2007


1aqe, resolution 2.2Å

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CRYSTAL STRUCTURE OF THE Y73E MUTANT OF CYTOCHROME C OF CLASS III (AMBLER) 26 KD

Overview

A combination of structural, kinetic, and interaction experiments has been, used to study the role of a highly conserved aromatic residue, Tyr73, parallel to the sixth heme axial ligand of heme 4 in multiheme cytochrome, c3 (Mr = 26 000), also called cytochrome cc3 or octaheme cytochrome, from, Desulfovibrio desulfuricans Norway. This residue is expected to be, involved in intermolecular electron transfer and protein-protein, interaction, since heme 4 is described to be the interaction site between, physiological partners. The kinetic experiments show that the Y73E, replacement provokes no significant change in the electron-transfer, reaction with the physiological partner, the [NiFeSe] hydrogenase, but, that the protein-protein interaction between cytochrome c3 (Mr = 26 000), and ... [(full description)]

About this Structure

1AQE is a [Single protein] structure of sequence from [Desulfovibrio desulfuricans] with SO4 and HEM as [ligands]. Structure known Active Sites: HE1, HE2, HE3 and HE4. Full crystallographic information is available from [OCA].

Reference

Structural and kinetic studies of the Y73E mutant of octaheme cytochrome c3 (Mr = 26 000) from Desulfovibrio desulfuricans Norway., Aubert C, Giudici-Orticoni MT, Czjzek M, Haser R, Bruschi M, Dolla A, Biochemistry. 1998 Feb 24;37(8):2120-30. PMID:9485359

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