Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases.
International audience Enzymes from psychrophilic organisms differ from their mesophilic counterparts in having a lower thermostability and a higher specific activity at low and moderate temperatures. It is in general accepted that psychrophilic enzymes are more flexible to allow easy accommodation...
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ftunivlyon1:oai:HAL:hal-00313543v1 2023-05-15T13:44:38+02:00 Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. Aghajari, N. Vanpetegem, F. Villeret, V. Chessa, Jp Gerday, C. Haser, R. Vanbeeumen, J. 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) 2003 https://hal.science/hal-00313543 en eng HAL CCSD Wiley hal-00313543 https://hal.science/hal-00313543 ISSN: 0887-3585 EISSN: 1097-0134 Proteins - Structure, Function and Bioinformatics https://hal.science/hal-00313543 Proteins - Structure, Function and Bioinformatics, 2003, 50, pp.636-647 [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology info:eu-repo/semantics/article Journal articles 2003 ftunivlyon1 2023-04-07T11:52:55Z International audience Enzymes from psychrophilic organisms differ from their mesophilic counterparts in having a lower thermostability and a higher specific activity at low and moderate temperatures. It is in general accepted that psychrophilic enzymes are more flexible to allow easy accommodation and transformation of the substrates at low energy costs. Here, we report the structures of two crystal forms of the alkaline protease from an Antarctic Pseudomonas species (PAP), solved to 2.1- and 1.96-A resolution, respectively. Comparative studies of PAP structures with mesophilic counterparts show that the overall structures are similar but that the conformation of the substrate-free active site in PAP resembles that of the substrate-bound region of the mesophilic homolog, with both an active-site tyrosine and a substrate-binding loop displaying a conformation as in the substrate-bound form of the mesophilic proteases. Further, a region in the catalytic domain of PAP undergoes a conformational change with a loop movement as large as 13 A, induced by the binding of an extra calcium ion. Finally, the active site is more accessible due to deletions occurring in surrounding loop regions.Enzymes from psychrophilic organisms differ from their mesophilic counterparts in having a lower thermostability and a higher specific activity at low and moderate temperatures. It is in general accepted that psychrophilic enzymes are more flexible to allow easy accommodation and transformation of the substrates at low energy costs. Here, we report the structures of two crystal forms of the alkaline protease from an Antarctic Pseudomonas species (PAP), solved to 2.1- and 1.96-A resolution, respectively. Comparative studies of PAP structures with mesophilic counterparts show that the overall structures are similar but that the conformation of the substrate-free active site in PAP resembles that of the substrate-bound region of the mesophilic homolog, with both an active-site tyrosine and a substrate-binding loop displaying a ... Article in Journal/Newspaper Antarc* Antarctic HAL Lyon 1 (University Claude Bernard Lyon 1) Antarctic |
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Open Polar |
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HAL Lyon 1 (University Claude Bernard Lyon 1) |
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ftunivlyon1 |
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English |
topic |
[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
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[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Aghajari, N. Vanpetegem, F. Villeret, V. Chessa, Jp Gerday, C. Haser, R. Vanbeeumen, J. Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. |
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[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
description |
International audience Enzymes from psychrophilic organisms differ from their mesophilic counterparts in having a lower thermostability and a higher specific activity at low and moderate temperatures. It is in general accepted that psychrophilic enzymes are more flexible to allow easy accommodation and transformation of the substrates at low energy costs. Here, we report the structures of two crystal forms of the alkaline protease from an Antarctic Pseudomonas species (PAP), solved to 2.1- and 1.96-A resolution, respectively. Comparative studies of PAP structures with mesophilic counterparts show that the overall structures are similar but that the conformation of the substrate-free active site in PAP resembles that of the substrate-bound region of the mesophilic homolog, with both an active-site tyrosine and a substrate-binding loop displaying a conformation as in the substrate-bound form of the mesophilic proteases. Further, a region in the catalytic domain of PAP undergoes a conformational change with a loop movement as large as 13 A, induced by the binding of an extra calcium ion. Finally, the active site is more accessible due to deletions occurring in surrounding loop regions.Enzymes from psychrophilic organisms differ from their mesophilic counterparts in having a lower thermostability and a higher specific activity at low and moderate temperatures. It is in general accepted that psychrophilic enzymes are more flexible to allow easy accommodation and transformation of the substrates at low energy costs. Here, we report the structures of two crystal forms of the alkaline protease from an Antarctic Pseudomonas species (PAP), solved to 2.1- and 1.96-A resolution, respectively. Comparative studies of PAP structures with mesophilic counterparts show that the overall structures are similar but that the conformation of the substrate-free active site in PAP resembles that of the substrate-bound region of the mesophilic homolog, with both an active-site tyrosine and a substrate-binding loop displaying 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 |
Aghajari, N. Vanpetegem, F. Villeret, V. Chessa, Jp Gerday, C. Haser, R. Vanbeeumen, J. |
author_facet |
Aghajari, N. Vanpetegem, F. Villeret, V. Chessa, Jp Gerday, C. Haser, R. Vanbeeumen, J. |
author_sort |
Aghajari, N. |
title |
Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. |
title_short |
Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. |
title_full |
Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. |
title_fullStr |
Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. |
title_full_unstemmed |
Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. |
title_sort |
crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. |
publisher |
HAL CCSD |
publishDate |
2003 |
url |
https://hal.science/hal-00313543 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
ISSN: 0887-3585 EISSN: 1097-0134 Proteins - Structure, Function and Bioinformatics https://hal.science/hal-00313543 Proteins - Structure, Function and Bioinformatics, 2003, 50, pp.636-647 |
op_relation |
hal-00313543 https://hal.science/hal-00313543 |
_version_ |
1766204268348440576 |