1JM1

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

Summary for 1JM1

• Entry DOI: 10.2210/pdb1jm1/pdb
• Descriptor: Rieske iron-sulfur protein soxF, MAGNESIUM ION, FE2/S2 (INORGANIC) CLUSTER, ... (4 entities in total)
• Functional Keywords: rieske iron-sulfur protein, electron transport, respiratory chain, oxidoreductase
• Biological source: Sulfolobus acidocaldarius
• Total number of polymer chains: 1
• Total formula weight: 21899.41

Authors

Boenisch, H.,Schmidt, C.L.,Schaefer, G.,Ladenstein, R. (deposition date: 2001-07-17, release date: 2002-07-17, Last modification date: 2024-11-13)

Primary citation

Bonisch, H.,Schmidt, C.L.,Schafer, G.,Ladenstein, R.
The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1.1 A resolution.
J.Mol.Biol., 319:791-805, 2002

PubMed Abstract: 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.

PubMed: 12054871
DOI: 10.1016/S0022-2836(02)00323-6

Experimental method

X-RAY DIFFRACTION (1.11 Å)