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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 |
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The Japan Academy
2004
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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. |
format | Online Article Text |
id | pubmed-8147672 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2004 |
publisher | The Japan Academy |
record_format | MEDLINE/PubMed |
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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