1jm1

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1jm1, resolution 1.11Å

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Crystal structure of the soluble domain of the Rieske protein II (soxF) from Sulfolobus acidocaldarius

Overview

The first crystal structure of an archaeal Rieske iron-sulfur protein, the, soluble domain of Rieske iron-sulfur protein II (soxF) from the, hyperthermo-acidophile Sulfolobus acidocaldarius, has been solved by, multiple wavelength anomalous dispersion (MAD) and has been refined to 1.1, A resolution. SoxF is a subunit of the terminal oxidase supercomplex SoxM, in the plasma membrane of S. acidocaldarius that combines features of a, cytochrome bc(1) complex and a cytochrome c oxidase. The [2Fe-2S] cluster, of soxF is most likely the primary electron acceptor during the oxidation, of caldariella quinone by the cytochrome a(587)/Rieske subcomplex. The, geometry of the [2Fe-2S] cluster and the structure of the cluster-binding, site are almost identical in soxF and the Rieske proteins from eucaryal, cytochrome bc(1) and b(6)f complexes, suggesting a strict conservation of, the catalytic mechanism. The main domain of soxF and part of the, cluster-binding domain, though structurally related, show a significantly, divergent structure with respect to topology, non-covalent interactions, and surface charges. The divergent structure of soxF reflects a different, topology of the soxM complex compared to eucaryal bc complexes and the, adaptation of the protein to the extreme ambient conditions on the outer, membrane surface of a hyperthermo-acidophilic organism.

About this Structure

1JM1 is a Single protein structure of sequence from Sulfolobus acidocaldarius with MG and FES as ligands. Full crystallographic information is available from OCA.

Reference

The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1.1 A resolution., Bonisch H, Schmidt CL, Schafer G, Ladenstein R, J Mol Biol. 2002 Jun 7;319(3):791-805. PMID:12054871

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