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Title: Increasing the electron-transfer ability of Cyanidioschyzon merolae ferredoxin by a one-point mutation – A high resolution and Fe-SAD phasing crystal structure analysis of the Asp58Asn mutant

Highlights: •A single amino acid change on the ferredoxin surface affects electron transfer. •Precise positions of amide atoms were located utilizing no prior structural data. •Ultra high resolution and SAD phasing may be used for bias-free model building. -- Abstract: Cyanidioschyzon merolae (Cm) is a single cell red algae that grows in rather thermophilic (40–50 °C) and acidic (pH 1–3) conditions. Ferredoxin (Fd) was purified from this algae and characterized as a plant-type [2Fe–2S] Fd by physicochemical techniques. A high resolution (0.97 Å) three-dimensional structure of the CmFd D58N mutant molecule has been determined using the Fe-SAD phasing method to clarify the precise position of the Asn58 amide, as this substitution increases the electron-transfer ability relative to wild-type CmFd by a factor of 1.5. The crystal structure reveals an electro-positive surface surrounding Asn58 that may interact with ferredoxin NADP{sup +} reductase or cytochrome c.
Authors:
 [1] ; ;  [2] ;  [1] ;  [3]
  1. Department of Life Science and Graduate School of Life Science, Rikkyo (St. Paul’s ) University, Toshima-ku, Tokyo 171-8501 (Japan)
  2. Application Laboratory, Rigaku Corporation, 3-9-12 Matsubara-cho, Akishima-shi, Tokyo 196-8666 (Japan)
  3. Research Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494 (Japan)
Publication Date:
OSTI Identifier:
22239669
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 436; Journal Issue: 4; Other Information: Copyright (c) 2013 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ALGAE; AMINO ACIDS; CRYSTAL STRUCTURE; ELECTRON TRANSFER; FERREDOXIN; GENE MUTATIONS; MUTANTS; NADP; PH VALUE