1gy2

From Proteopedia

Revision as of 14:17, 5 November 2007

CRYSTAL STRUCTURE OF MET148LEU RUSTICYANIN

Overview

The crystal structures of the Met148Leu and Ser86Asp mutants of, rusticyanin are presented at 1.82 and 1.65 A resolution, respectively., Both of these structures have two molecules in the asymmetric unit, compared to the one present in the crystal form of the native protein., This provides an opportunity to investigate intramolecular electron, transfer pathways in rusticyanin. The redox potential of the Met148Leu, mutant ( approximately 800 mV) is elevated compared to that of the native, protein ( approximately 670 mV at pH 3.2) while that of the Ser86Asp, mutant ( approximately 623 mV at pH 3.2) is decreased. The effect of the, Ser86Asp mutation on the hydrogen bonding near the type 1 Cu site is, discussed and hence its role in determining acid stability is examined., The type 1 Cu site of Met148Leu mimics the structural and biochemical, characteristics of those found in domain II of ceruloplasmin and fungal, laccase. Moreover, the native rusticyanin's cupredoxin core and the type 1, Cu site closely resemble those found in ascorbate oxidase and nitrite, reductase. Structure based phylogenetic trees have been re-examined in, view of the additional structural data on rusticyanin and fungal laccase., We confirm that rusticyanin is in the same class as nitrite reductase, domain 2, laccase domain 3 and ceruloplasmin domains 2, 4 and 6.

About this Structure

1GY2 is a Single protein structure of sequence from Acidithiobacillus ferrooxidans with CU and GOL as ligands. Structure known Active Site: CUA. Full crystallographic information is available from OCA.

Reference

Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: insights into the structural relationship with the cupredoxins and the multi copper proteins., Kanbi LD, Antonyuk S, Hough MA, Hall JF, Dodd FE, Hasnain SS, J Mol Biol. 2002 Jul 5;320(2):263-75. PMID:12079384

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