2VPX

Polysulfide reductase with bound quinone (UQ1)

Summary for 2VPX

• Entry DOI: 10.2210/pdb2vpx/pdb
• Related: 2VPW 2VPY 2VPZ
• Descriptor: THIOSULFATE REDUCTASE, NRFC PROTEIN, HYPOTHETICAL MEMBRANE SPANNING PROTEIN, ... (8 entities in total)
• Functional Keywords: oxidoreductase, molybdenum, molybdopterin, mpt, molybdopterin guanine dinucleotide, mgd, iron sulfur cluster, fe4s4, integral membrane protein
• Biological source: THERMUS THERMOPHILUS; More
• Total number of polymer chains: 6
• Total formula weight: 278705.48

Authors

Jormakka, M.,Yokoyama, K.,Yano, T.,Tamakoshi, M.,Akimoto, S.,Shimamura, T.,Curmi, P.,Iwata, S. (deposition date: 2008-03-09, release date: 2008-06-10, Last modification date: 2011-07-13)

Primary citation

Jormakka, M.,Yokoyama, K.,Yano, T.,Tamakoshi, M.,Akimoto, S.,Shimamura, T.,Curmi, P.,Iwata, S.
Molecular Mechanism of Energy Conservation in Polysulfide Respiration.
Nat.Struct.Mol.Biol., 15:730-, 2008

PubMed Abstract: Bacterial polysulfide reductase (PsrABC) is an integral membrane protein complex responsible for quinone-coupled reduction of polysulfide, a process important in extreme environments such as deep-sea vents and hot springs. We determined the structure of polysulfide reductase from Thermus thermophilus at 2.4-A resolution, revealing how the PsrA subunit recognizes and reduces its unique polyanionic substrate. The integral membrane subunit PsrC was characterized using the natural substrate menaquinone-7 and inhibitors, providing a comprehensive representation of a quinone binding site and revealing the presence of a water-filled cavity connecting the quinone binding site on the periplasmic side to the cytoplasm. These results suggest that polysulfide reductase could be a key energy-conserving enzyme of the T. thermophilus respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane via a previously unknown mechanism.

PubMed: 18536726
DOI: 10.1038/NSMB.1434

Experimental method

X-RAY DIFFRACTION (3.1 Å)