Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase.
International audience The glycolytic enzyme phosphoglycerate kinase (PGK) from the Antarctic microorganism Pseudomonas sp. TACII18 is a cold-adapted enzyme that displays a high specific activity at low temperatures and decreased thermostability relative to its mesophilic counterpart. Herein, the pr...
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ftunivnantes:oai:HAL:hal-00313550v1 2023-05-15T13:51:43+02:00 Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase. Mandelman, D. Bentahir, M. Feller, G. Gerday, C. Haser, R. Institut de biologie et chimie des protéines Lyon (IBCP) Université Claude Bernard Lyon 1 (UCBL) Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS) 2001 https://hal.science/hal-00313550 en eng HAL CCSD hal-00313550 https://hal.science/hal-00313550 Acta Crystallogr D Biol Crystallogr https://hal.science/hal-00313550 Acta Crystallogr D Biol Crystallogr, 2001, 57, pp.1666-1668 [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology info:eu-repo/semantics/article Journal articles 2001 ftunivnantes 2023-02-08T04:51:25Z International audience The glycolytic enzyme phosphoglycerate kinase (PGK) from the Antarctic microorganism Pseudomonas sp. TACII18 is a cold-adapted enzyme that displays a high specific activity at low temperatures and decreased thermostability relative to its mesophilic counterpart. Herein, the preliminary crystallization and structure solution of psychrophilic PGK in its native form and cocrystallized with 3-phosphoglyceric acid (3-PGA) and the ATP analogue adenylyl imidophosphate (AMP-PNP) is reported. The complexed form of PGK crystallized in 2-3 d at 290 K, whereas the native form of the enzyme required 8-12 months. Morphologically, both crystal forms are similar and X-ray diffraction experiments indicate that the crystals are isomorphous. The crystals diffracted to a resolution of 2.0 A and belong to the space group P3(2). with unit-cell parameters a = b = 58.5, c = 85.4 A.The glycolytic enzyme phosphoglycerate kinase (PGK) from the Antarctic microorganism Pseudomonas sp. TACII18 is a cold-adapted enzyme that displays a high specific activity at low temperatures and decreased thermostability relative to its mesophilic counterpart. Herein, the preliminary crystallization and structure solution of psychrophilic PGK in its native form and cocrystallized with 3-phosphoglyceric acid (3-PGA) and the ATP analogue adenylyl imidophosphate (AMP-PNP) is reported. The complexed form of PGK crystallized in 2-3 d at 290 K, whereas the native form of the enzyme required 8-12 months. Morphologically, both crystal forms are similar and X-ray diffraction experiments indicate that the crystals are isomorphous. The crystals diffracted to a resolution of 2.0 A and belong to the space group P3(2). with unit-cell parameters a = b = 58.5, c = 85.4 A. Article in Journal/Newspaper Antarc* Antarctic Université de Nantes: HAL-UNIV-NANTES Antarctic The Antarctic |
institution |
Open Polar |
collection |
Université de Nantes: HAL-UNIV-NANTES |
op_collection_id |
ftunivnantes |
language |
English |
topic |
[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
spellingShingle |
[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Mandelman, D. Bentahir, M. Feller, G. Gerday, C. Haser, R. Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase. |
topic_facet |
[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
description |
International audience The glycolytic enzyme phosphoglycerate kinase (PGK) from the Antarctic microorganism Pseudomonas sp. TACII18 is a cold-adapted enzyme that displays a high specific activity at low temperatures and decreased thermostability relative to its mesophilic counterpart. Herein, the preliminary crystallization and structure solution of psychrophilic PGK in its native form and cocrystallized with 3-phosphoglyceric acid (3-PGA) and the ATP analogue adenylyl imidophosphate (AMP-PNP) is reported. The complexed form of PGK crystallized in 2-3 d at 290 K, whereas the native form of the enzyme required 8-12 months. Morphologically, both crystal forms are similar and X-ray diffraction experiments indicate that the crystals are isomorphous. The crystals diffracted to a resolution of 2.0 A and belong to the space group P3(2). with unit-cell parameters a = b = 58.5, c = 85.4 A.The glycolytic enzyme phosphoglycerate kinase (PGK) from the Antarctic microorganism Pseudomonas sp. TACII18 is a cold-adapted enzyme that displays a high specific activity at low temperatures and decreased thermostability relative to its mesophilic counterpart. Herein, the preliminary crystallization and structure solution of psychrophilic PGK in its native form and cocrystallized with 3-phosphoglyceric acid (3-PGA) and the ATP analogue adenylyl imidophosphate (AMP-PNP) is reported. The complexed form of PGK crystallized in 2-3 d at 290 K, whereas the native form of the enzyme required 8-12 months. Morphologically, both crystal forms are similar and X-ray diffraction experiments indicate that the crystals are isomorphous. The crystals diffracted to a resolution of 2.0 A and belong to the space group P3(2). with unit-cell parameters a = b = 58.5, c = 85.4 A. |
author2 |
Institut de biologie et chimie des protéines Lyon (IBCP) Université Claude Bernard Lyon 1 (UCBL) Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS) |
format |
Article in Journal/Newspaper |
author |
Mandelman, D. Bentahir, M. Feller, G. Gerday, C. Haser, R. |
author_facet |
Mandelman, D. Bentahir, M. Feller, G. Gerday, C. Haser, R. |
author_sort |
Mandelman, D. |
title |
Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase. |
title_short |
Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase. |
title_full |
Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase. |
title_fullStr |
Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase. |
title_full_unstemmed |
Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase. |
title_sort |
crystallization and preliminary x-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase. |
publisher |
HAL CCSD |
publishDate |
2001 |
url |
https://hal.science/hal-00313550 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Acta Crystallogr D Biol Crystallogr https://hal.science/hal-00313550 Acta Crystallogr D Biol Crystallogr, 2001, 57, pp.1666-1668 |
op_relation |
hal-00313550 https://hal.science/hal-00313550 |
_version_ |
1766255755603738624 |