Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12
Fuculose-1-phosphate aldolase (FucA) catalyses the reversible cleavage of l-fuculose 1-phosphate to dihydroxyacetone phosphate (DHAP) and l-lactaldehyde. This enzyme from mesophiles and thermophiles has been extensively studied; however, there is no report on this enzyme from a psychrophile. In this...
Published in: | Acta Crystallographica Section F Structural Biology Communications |
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ftunivmalaysia:oai:generic.eprints.org:69116 2023-05-15T13:54:23+02:00 Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12 Jaafar, Nardiah Rizwana Littler, Dene Beddoe, Travis Rossjohn, Jamie Md. Illias, Rosli Mahadi, Nor Muhammad Mackeen, Mukram Mohamed Abdul Murad, Abdul Munir Abu Bakar, Farah Diba 2016 http://eprints.utm.my/69116/ https://doi.org/10.1107/S2053230X16015612 unknown International Union of Crystallography Jaafar, Nardiah Rizwana and Littler, Dene and Beddoe, Travis and Rossjohn, Jamie and Md. Illias, Rosli and Mahadi, Nor Muhammad and Mackeen, Mukram Mohamed and Abdul Murad, Abdul Munir and Abu Bakar, Farah Diba (2016) Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12. Acta Crystallographica Section:F Structural Biology Communications, 72 (11). pp. 831-839. ISSN 2053-230X TP Chemical technology Article PeerReviewed 2016 ftunivmalaysia https://doi.org/10.1107/S2053230X16015612 2017-11-21T15:57:15Z Fuculose-1-phosphate aldolase (FucA) catalyses the reversible cleavage of l-fuculose 1-phosphate to dihydroxyacetone phosphate (DHAP) and l-lactaldehyde. This enzyme from mesophiles and thermophiles has been extensively studied; however, there is no report on this enzyme from a psychrophile. In this study, the gene encoding FucA from Glaciozyma antarctica PI12 (GaFucA) was cloned and the enzyme was overexpressed in Escherichia coli, purified and crystallized. The tetrameric structure of GaFucA was determined to 1.34 Å resolution. The overall architecture of GaFucA and its catalytically essential histidine triad are highly conserved among other fuculose aldolases. Comparisons of structural features between GaFucA and its mesophilic and thermophilic homologues revealed that the enzyme has typical psychrophilic attributes, indicated by the presence of a high number of nonpolar residues at the surface and a lower number of arginine residues. Article in Journal/Newspaper Antarc* Antarctic Antarctica Universiti Teknologi Malaysia: Institutional Repository Antarctic The Antarctic Acta Crystallographica Section F Structural Biology Communications 72 11 831 839 |
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Universiti Teknologi Malaysia: Institutional Repository |
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TP Chemical technology |
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TP Chemical technology Jaafar, Nardiah Rizwana Littler, Dene Beddoe, Travis Rossjohn, Jamie Md. Illias, Rosli Mahadi, Nor Muhammad Mackeen, Mukram Mohamed Abdul Murad, Abdul Munir Abu Bakar, Farah Diba Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12 |
topic_facet |
TP Chemical technology |
description |
Fuculose-1-phosphate aldolase (FucA) catalyses the reversible cleavage of l-fuculose 1-phosphate to dihydroxyacetone phosphate (DHAP) and l-lactaldehyde. This enzyme from mesophiles and thermophiles has been extensively studied; however, there is no report on this enzyme from a psychrophile. In this study, the gene encoding FucA from Glaciozyma antarctica PI12 (GaFucA) was cloned and the enzyme was overexpressed in Escherichia coli, purified and crystallized. The tetrameric structure of GaFucA was determined to 1.34 Å resolution. The overall architecture of GaFucA and its catalytically essential histidine triad are highly conserved among other fuculose aldolases. Comparisons of structural features between GaFucA and its mesophilic and thermophilic homologues revealed that the enzyme has typical psychrophilic attributes, indicated by the presence of a high number of nonpolar residues at the surface and a lower number of arginine residues. |
format |
Article in Journal/Newspaper |
author |
Jaafar, Nardiah Rizwana Littler, Dene Beddoe, Travis Rossjohn, Jamie Md. Illias, Rosli Mahadi, Nor Muhammad Mackeen, Mukram Mohamed Abdul Murad, Abdul Munir Abu Bakar, Farah Diba |
author_facet |
Jaafar, Nardiah Rizwana Littler, Dene Beddoe, Travis Rossjohn, Jamie Md. Illias, Rosli Mahadi, Nor Muhammad Mackeen, Mukram Mohamed Abdul Murad, Abdul Munir Abu Bakar, Farah Diba |
author_sort |
Jaafar, Nardiah Rizwana |
title |
Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12 |
title_short |
Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12 |
title_full |
Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12 |
title_fullStr |
Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12 |
title_full_unstemmed |
Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12 |
title_sort |
crystal structure of fuculose aldolase from the antarctic psychrophilic yeast glaciozyma antarctica pi12 |
publisher |
International Union of Crystallography |
publishDate |
2016 |
url |
http://eprints.utm.my/69116/ https://doi.org/10.1107/S2053230X16015612 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Antarctica |
genre_facet |
Antarc* Antarctic Antarctica |
op_relation |
Jaafar, Nardiah Rizwana and Littler, Dene and Beddoe, Travis and Rossjohn, Jamie and Md. Illias, Rosli and Mahadi, Nor Muhammad and Mackeen, Mukram Mohamed and Abdul Murad, Abdul Munir and Abu Bakar, Farah Diba (2016) Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12. Acta Crystallographica Section:F Structural Biology Communications, 72 (11). pp. 831-839. ISSN 2053-230X |
op_doi |
https://doi.org/10.1107/S2053230X16015612 |
container_title |
Acta Crystallographica Section F Structural Biology Communications |
container_volume |
72 |
container_issue |
11 |
container_start_page |
831 |
op_container_end_page |
839 |
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1766260135795097600 |