2bh5
X-RAY STRUCTURE OF THE M100K VARIANT OF FERRIC CYT C-550 FROM PARACOCCUS VERSUTUS DETERMINED AT 295 K.
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OverviewOverview
The structure of cytochrome c-550 from the nonphotosynthetic bacteria, Paraccocus versutus has been solved by X-ray crystallography to 1.90 A, resolution, and reveals a high structural homology to other bacterial, cytochromes c(2). The effect of replacing the axial heme-iron methionine, ligand with a lysine residue on protein structure and unfolding has been, assessed using the M100K variant. From X-ray structures at 1.95 and 1.55 A, resolution it became clear that the amino group of the lysine side chain, coordinates to the heme-iron. Structural differences compared to the, wild-type protein are confined to the lysine ligand loop connecting, helices four and five. In the heme cavity an additional water molecule is, found which participates in an H-bonding interaction with the lysine, ... [(full description)]
About this StructureAbout this Structure
2BH5 is a [Single protein] structure of sequence from [Paracoccus versutus] with HEC as [ligand]. Full crystallographic information is available from [OCA].
ReferenceReference
The effect of replacing the axial methionine ligand with a lysine residue in cytochrome c-550 from Paracoccus versutus assessed by X-ray crystallography and unfolding., Worrall JA, van Roon AM, Ubbink M, Canters GW, FEBS J. 2005 May;272(10):2441-55. PMID:15885094
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