Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 390, Issue 3, Pages 597-602Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.10.012
Keywords
Zeta-crystallin; Quinone oxidoreductase; NADPH; Crystal structure; Conformational change
Categories
Funding
- National Natural Science Foundation of China [30530210, 30721003]
- Chinese Academy of Sciences [KSCX2-YW-R-123]
- 973 Project [2006CB806505, 2006CB911001]
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Zeta-crystallin-like quinone oxidoreductase is NAD(P)H-dependent and catalyzes one-electron reduction of certain quinones to generate semiquinone. Here we present the crystal structures of zeta-crystallin-like quinone oxidoreductase from Pseudomonas syringae pv, tomato DC3000 (PtoQOR) and its complexes with NADPH determined at 2.4 and 2.01 angstrom resolutions, respectively. PtoQOR forms as a homologous dimer, each monomer containing two domains. In the Structure of the PtoQOR-NADPH complex, NADPH locates in the groove between the two domains. NADPH binding causes obvious conformational changes in the structure of PtoQOR. The putative substrate-binding site of PtoQOR is wider than that of Escherichia coli and Thermus thermophilus HB8. Activity assays show that PtoQOR has weak 1,4-benzoquinone catalytic activity, and very strong reduction activity towards large substrates such as 9,10-phenanthrenequinone. We propose a model to explain the conformational changes which take place during reduction reactions catalyzed by PtoQOR. (C) 2009 Published by Elsevier Inc.
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