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Molecular mechanism of energy conservation in polysulfide respiration
Authors:
M.
Jormakka
(University of New South Wales; Centenary Institute of Cancer Medicine and Cell Biology (Australia); University of Sydney)
,
K.
Yokoyama
(Tokyo Institute of Technology; Japan Science and Technology Agency)
,
S.
Yano
(Japan Science and Technology Agency)
,
M.
Tamakoshi
(Tokyo University of Pharmacy and Life Science)
,
S.
Akimoto
(Japan Science and Technology Agency)
,
T.
Shimamura
(RIKEN SPring-8 Center; Japan Science and Technology Agency)
,
P.
Curmi
(University of New South Wales)
,
S.
Iwata
(Japan Science and Technology Agency; Imperial College London; RIKEN Genomic Sciences Center,)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Nature Structural & Molecular Biology
, VOL 15 (7)
, PAGES 730 - 737
State:
Published (Approved)
Published:
June 2008
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-Å 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.
Diamond Keywords: Bacteria
Subject Areas:
Biology and Bio-materials
Diamond Offline Facilities:
Membrane Protein Laboratory (MPL)
Instruments:
NONE-No attached Diamond beamline
Added On:
19/08/2009 23:07
Discipline Tags:
Structural biology
Life Sciences & Biotech
Technical Tags: