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Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3
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 resolut...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Japan Academy
2004
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8147672/ |
Sumario: | 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 P3(2)21, 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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