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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...

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Autores principales: Miyazono, Ken-ichi, Sawano, Yoriko, Tanokura, Masaru
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Japan Academy 2004
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8147672/
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author Miyazono, Ken-ichi
Sawano, Yoriko
Tanokura, Masaru
author_facet Miyazono, Ken-ichi
Sawano, Yoriko
Tanokura, Masaru
author_sort Miyazono, Ken-ichi
collection PubMed
description 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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spelling pubmed-81476722021-05-28 Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3 Miyazono, Ken-ichi Sawano, Yoriko Tanokura, Masaru Proc Jpn Acad Ser B Phys Biol Sci Articles 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. The Japan Academy 2004-09 2004-09-01 /pmc/articles/PMC8147672/ Text en © 2004 The Japan Academy https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Articles
Miyazono, Ken-ichi
Sawano, Yoriko
Tanokura, Masaru
Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3
title Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3
title_full Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3
title_fullStr Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3
title_full_unstemmed Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3
title_short Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3
title_sort crystal structure of acylphosphatase from hyperthermophilic archaeon pyrococcus horikoshii ot3
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8147672/
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