3H31

Structure of Rhodothermus marinus HiPIP at 1.0 A resolution

Summary for 3H31

• Entry DOI: 10.2210/pdb3h31/pdb
• Descriptor: High potential iron-sulfur protein, IRON/SULFUR CLUSTER (3 entities in total)
• Functional Keywords: iron-sulfur protein, electron transport, iron, metal-binding, transport
• Biological source: Rhodothermus marinus
• Total number of polymer chains: 1
• Total formula weight: 8451.65

Authors

Stelter, M.,Melo, A.M.P.,Saraiva, L.,Teixeira, M.,Archer, M. (deposition date: 2009-04-15, release date: 2009-12-15, Last modification date: 2018-01-24)

Primary citation

Stelter, M.,Melo, A.M.P.,Hreggvidsson, G.O.,Hjorleifsdottir, S.,Saraiva, L.M.,Teixeira, M.,Archer, M.
Structure at 1.0 A resolution of a high-potential iron-sulfur protein involved in the aerobic respiratory chain of Rhodothermus marinus
J.Biol.Inorg.Chem., 15:303-313, 2010

PubMed Abstract: The aerobic respiratory chain of the thermohalophilic bacterium Rhodothermus marinus, a nonphotosynthetic organism from the Bacteroidetes/Chlorobi group, contains a high-potential iron-sulfur protein (HiPIP) that transfers electrons from a bc 1 analog complex to a caa 3 oxygen reductase. Here, we describe the crystal structure of the reduced form of R. marinus HiPIP, solved by the single-wavelength anomalous diffraction method, based on the anomalous scattering of the iron atoms from the [4Fe-4S]3+/2+ cluster and refined to 1.0 A resolution. This is the first structure of a HiPIP isolated from a nonphotosynthetic bacterium involved in an aerobic respiratory chain. The structure shows a similar environment around the cluster as the other HiPIPs from phototrophic bacteria, but reveals several features distinct from those of the other HiPIPs of phototrophic bacteria, such as a different fold of the N-terminal region of the polypeptide due to a disulfide bridge and a ten-residue-long insertion.

PubMed: 20225399
DOI: 10.1007/s00775-009-0603-8

Experimental method

X-RAY DIFFRACTION (1 Å)