Stability domains, substrate-induced conformational changes, and hinge-bending motions in a psychrophilic phosphoglycerate kinase: A microcalorimetric study
peer reviewed The cold-active phosphoglycerate kinase from the Antarctic bacterium Pseudomonas sp. TACII18 exhibits two distinct stability domains in the free, open conformation. It is shown that these stability domains do not match the structural N- and C-domains as the heat-stable domain correspon...
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Amer Soc Biochemistry Molecular Biology Inc
2005
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ftorbi:oai:orbi.ulg.ac.be:2268/15405 2024-04-21T07:50:04+00:00 Stability domains, substrate-induced conformational changes, and hinge-bending motions in a psychrophilic phosphoglycerate kinase: A microcalorimetric study Zecchinon, Laurent Oriol, A. Netzel, U. Svennberg, J. Gerardin-Otthiers, N. Feller, Georges 2005-12-16 https://orbi.uliege.be/handle/2268/15405 https://orbi.uliege.be/bitstream/2268/15405/1/JBC_2005_PGK.pdf https://doi.org/10.1074/jbc.M506464200 en eng Amer Soc Biochemistry Molecular Biology Inc urn:issn:0021-9258 urn:issn:1083-351X https://orbi.uliege.be/handle/2268/15405 info:hdl:2268/15405 https://orbi.uliege.be/bitstream/2268/15405/1/JBC_2005_PGK.pdf doi:10.1074/jbc.M506464200 scopus-id:2-s2.0-29244485572 info:pmid:16227206 open access http://purl.org/coar/access_right/c_abf2 info:eu-repo/semantics/openAccess Journal of Biological Chemistry, 280 (50), 41307-41314 (2005-12-16) Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire journal article http://purl.org/coar/resource_type/c_6501 info:eu-repo/semantics/article peer reviewed 2005 ftorbi https://doi.org/10.1074/jbc.M506464200 2024-03-27T14:52:24Z peer reviewed The cold-active phosphoglycerate kinase from the Antarctic bacterium Pseudomonas sp. TACII18 exhibits two distinct stability domains in the free, open conformation. It is shown that these stability domains do not match the structural N- and C-domains as the heat-stable domain corresponds to about 80 residues of the C-domain, including the nucleotide binding site, whereas the remaining of the protein contributes to the main heat-labile domain. This was demonstrated by spectroscopic and microcalorimetric analyses of the native enzyme, of its mutants, and of the isolated recombinant structural domains. It is proposed that the heat-stable domain provides a compact structure improving the binding affinity of the nucleotide, therefore increasing the catalytic efficiency at low temperatures. Upon substrate binding, the enzyme adopts a uniformly more stable closed conformation. Substrate-induced stability changes suggest that the free energy of ligand binding is converted into an increased conformational stability used to drive the hinge-bending motions and domain closure. Article in Journal/Newspaper Antarc* Antarctic University of Liège: ORBi (Open Repository and Bibliography) Journal of Biological Chemistry 280 50 41307 41314 |
institution |
Open Polar |
collection |
University of Liège: ORBi (Open Repository and Bibliography) |
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ftorbi |
language |
English |
topic |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
spellingShingle |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire Zecchinon, Laurent Oriol, A. Netzel, U. Svennberg, J. Gerardin-Otthiers, N. Feller, Georges Stability domains, substrate-induced conformational changes, and hinge-bending motions in a psychrophilic phosphoglycerate kinase: A microcalorimetric study |
topic_facet |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
description |
peer reviewed The cold-active phosphoglycerate kinase from the Antarctic bacterium Pseudomonas sp. TACII18 exhibits two distinct stability domains in the free, open conformation. It is shown that these stability domains do not match the structural N- and C-domains as the heat-stable domain corresponds to about 80 residues of the C-domain, including the nucleotide binding site, whereas the remaining of the protein contributes to the main heat-labile domain. This was demonstrated by spectroscopic and microcalorimetric analyses of the native enzyme, of its mutants, and of the isolated recombinant structural domains. It is proposed that the heat-stable domain provides a compact structure improving the binding affinity of the nucleotide, therefore increasing the catalytic efficiency at low temperatures. Upon substrate binding, the enzyme adopts a uniformly more stable closed conformation. Substrate-induced stability changes suggest that the free energy of ligand binding is converted into an increased conformational stability used to drive the hinge-bending motions and domain closure. |
format |
Article in Journal/Newspaper |
author |
Zecchinon, Laurent Oriol, A. Netzel, U. Svennberg, J. Gerardin-Otthiers, N. Feller, Georges |
author_facet |
Zecchinon, Laurent Oriol, A. Netzel, U. Svennberg, J. Gerardin-Otthiers, N. Feller, Georges |
author_sort |
Zecchinon, Laurent |
title |
Stability domains, substrate-induced conformational changes, and hinge-bending motions in a psychrophilic phosphoglycerate kinase: A microcalorimetric study |
title_short |
Stability domains, substrate-induced conformational changes, and hinge-bending motions in a psychrophilic phosphoglycerate kinase: A microcalorimetric study |
title_full |
Stability domains, substrate-induced conformational changes, and hinge-bending motions in a psychrophilic phosphoglycerate kinase: A microcalorimetric study |
title_fullStr |
Stability domains, substrate-induced conformational changes, and hinge-bending motions in a psychrophilic phosphoglycerate kinase: A microcalorimetric study |
title_full_unstemmed |
Stability domains, substrate-induced conformational changes, and hinge-bending motions in a psychrophilic phosphoglycerate kinase: A microcalorimetric study |
title_sort |
stability domains, substrate-induced conformational changes, and hinge-bending motions in a psychrophilic phosphoglycerate kinase: a microcalorimetric study |
publisher |
Amer Soc Biochemistry Molecular Biology Inc |
publishDate |
2005 |
url |
https://orbi.uliege.be/handle/2268/15405 https://orbi.uliege.be/bitstream/2268/15405/1/JBC_2005_PGK.pdf https://doi.org/10.1074/jbc.M506464200 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Journal of Biological Chemistry, 280 (50), 41307-41314 (2005-12-16) |
op_relation |
urn:issn:0021-9258 urn:issn:1083-351X https://orbi.uliege.be/handle/2268/15405 info:hdl:2268/15405 https://orbi.uliege.be/bitstream/2268/15405/1/JBC_2005_PGK.pdf doi:10.1074/jbc.M506464200 scopus-id:2-s2.0-29244485572 info:pmid:16227206 |
op_rights |
open access http://purl.org/coar/access_right/c_abf2 info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1074/jbc.M506464200 |
container_title |
Journal of Biological Chemistry |
container_volume |
280 |
container_issue |
50 |
container_start_page |
41307 |
op_container_end_page |
41314 |
_version_ |
1796933937531977728 |