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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.

Ueno Y, Matsumoto T, Yamano A, Imai T, Morimoto Y
Biochem Biophys Res Commun 436 736-9 (2013)
Cited: 3 times
EuropePMC logo PMID: 23792094

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 (0.97Å) 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(+) reductase or cytochrome c.

Articles - 3wcq mentioned but not cited (3)

  1. Reciprocal carbonyl-carbonyl interactions in small molecules and proteins. Rahim A, Saha P, Jha KK, Sukumar N, Sarma BK. Nat Commun 8 78 (2017)
  2. Accuracy issues involved in modeling in vivo protein structures using PM7. Martin BP, Brandon CJ, Stewart JJ, Braun-Sand SB. Proteins 83 1427-1435 (2015)
  3. The oxygen-oxygen distance of water in crystallographic data sets. Palese LL. Data Brief 28 105076 (2020)




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