Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold‐adapted proteases
Abstract 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 transforma...
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crwiley:10.1002/prot.10264 2024-09-15T17:41:20+00:00 Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold‐adapted proteases Aghajari, Nushin Van Petegem, Filip Villeret, Vincent Chessa, Jean‐Pierre Gerday, Charles Haser, Richard Van Beeumen, Jozef 2003 http://dx.doi.org/10.1002/prot.10264 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.10264 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.10264 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Proteins: Structure, Function, and Bioinformatics volume 50, issue 4, page 636-647 ISSN 0887-3585 1097-0134 journal-article 2003 crwiley https://doi.org/10.1002/prot.10264 2024-08-06T04:15:03Z Abstract 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‐Å 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 Å, induced by the binding of an extra calcium ion. Finally, the active site is more accessible due to deletions occurring in surrounding loop regions. Proteins 2003;50:636–647. © 2003 Wiley‐Liss, Inc. Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library Proteins: Structure, Function, and Bioinformatics 50 4 636 647 |
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Wiley Online Library |
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English |
description |
Abstract 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‐Å 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 Å, induced by the binding of an extra calcium ion. Finally, the active site is more accessible due to deletions occurring in surrounding loop regions. Proteins 2003;50:636–647. © 2003 Wiley‐Liss, Inc. |
format |
Article in Journal/Newspaper |
author |
Aghajari, Nushin Van Petegem, Filip Villeret, Vincent Chessa, Jean‐Pierre Gerday, Charles Haser, Richard Van Beeumen, Jozef |
spellingShingle |
Aghajari, Nushin Van Petegem, Filip Villeret, Vincent Chessa, Jean‐Pierre Gerday, Charles Haser, Richard Van Beeumen, Jozef Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold‐adapted proteases |
author_facet |
Aghajari, Nushin Van Petegem, Filip Villeret, Vincent Chessa, Jean‐Pierre Gerday, Charles Haser, Richard Van Beeumen, Jozef |
author_sort |
Aghajari, Nushin |
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 |
Wiley |
publishDate |
2003 |
url |
http://dx.doi.org/10.1002/prot.10264 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.10264 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.10264 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Proteins: Structure, Function, and Bioinformatics volume 50, issue 4, page 636-647 ISSN 0887-3585 1097-0134 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/prot.10264 |
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Proteins: Structure, Function, and Bioinformatics |
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50 |
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4 |
container_start_page |
636 |
op_container_end_page |
647 |
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1810487489358462976 |