1vyd
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CRYSTAL STRUCTURE OF CYTOCHROME C2 MUTANT G95E
OverviewOverview
All class I c-type cytochromes studied to date undergo a dynamic process, in the oxidized state, which results in the transient breaking of the, iron-methionine-sulfur bond and sufficient movement to allow the binding, of exogenous ligands (imidazole in this work). In the case of Rhodobacter, capsulatus cytochrome c(2), the sixth heme ligand Met96 and up to 14, flanking residues (positions 88-100, termed the hinge region), located, between two relatively rigid helical regions, may be involved in, structural changes leading to a transient high-spin species able to bind, ligands. We have examined 14 mutations at 9 positions in the hinge region, of Rhodobacter capsulatus cytochrome c(2) and have determined the, structure of the G95E mutant. Mutations near the N- and C-terminus of the, hinge ... [(full description)]
About this StructureAbout this Structure
1VYD is a [Single protein] structure of sequence from [Rhodobacter capsulatus] with HEM as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Protein dynamics in the region of the sixth ligand methionine revealed by studies of imidazole binding to Rhodobacter capsulatus cytochrome c2 hinge mutants., Dumortier C, Fitch J, Van Petegem F, Vermeulen W, Meyer TE, Van Beeumen JJ, Cusanovich MA, Biochemistry. 2004 Jun 22;43(24):7717-24. PMID:15196014
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