Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3

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Abstract

Analysis of the hyperthermophilic archaeon Pyrococcus horikoshii OT3 genome database led to the discovery and cloning of acylphosphatase (ORF PH0305a). To elucidate the first structure of archaeal acylphosphatase, we determined the crystal structure of P. horikoshii acylphosphatase at 1.72 Å resolution. The space group of the crystals was P3221, with unit-cell parameters a = b = 86.6 Å and c = 75.4 Å. The overall fold of P. horikoshii acylphosphatase was very similar to the structures of the eukaryotic enzymes. The conformation of putative active site was highly conserved.

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Miyazono, K. I., Sawano, Y., & Tanokura, M. (2004). Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3. Proceedings of the Japan Academy Series B: Physical and Biological Sciences, 80(9), 439–442. https://doi.org/10.2183/pjab.80.439

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