Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis
Superoxide dismutases (SODs) are metalloenzymes catalysing the dismutation of superoxide anion radicals into molecular oxygen and hydrogen peroxide. Here, we present the crystal structure of a cold-adapted Fe-SOD from the Antarctic eubacterium Pseudoalteromonas haloplanktis (PhSOD), and that of its...
Published in: | Journal of Structural Biology |
---|---|
Main Authors: | , , , , , , , |
Other Authors: | , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
2010
|
Subjects: | |
Online Access: | http://hdl.handle.net/11588/371041 https://doi.org/10.1016/j.jsb.2010.08.008 http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WM5-50V20D3-2&_user=2607107&_coverDate=08%2F21%2F2010&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_acct=C000057976&_version=1&_urlVersion=0&_userid=2607107&md5=5261f061e0e3a5fbdec45a1a4d974192&searchtype=a |
id |
ftunivnapoliiris:oai:www.iris.unina.it:11588/371041 |
---|---|
record_format |
openpolar |
spelling |
ftunivnapoliiris:oai:www.iris.unina.it:11588/371041 2024-09-09T19:08:56+00:00 Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis MERLINO, ANTONELLO RUSSO KRAUSS, IRENE CASTELLANO, IMMACOLATA DE VENDITTIS, EMMANUELE VERGARA, ALESSANDRO SICA, FILOMENA B. Rossi M. Conte Merlino, Antonello RUSSO KRAUSS, Irene Castellano, Immacolata DE VENDITTIS, Emmanuele B., Rossi M., Conte Vergara, Alessandro Sica, Filomena 2010 STAMPA http://hdl.handle.net/11588/371041 https://doi.org/10.1016/j.jsb.2010.08.008 http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WM5-50V20D3-2&_user=2607107&_coverDate=08%2F21%2F2010&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_acct=C000057976&_version=1&_urlVersion=0&_userid=2607107&md5=5261f061e0e3a5fbdec45a1a4d974192&searchtype=a eng eng info:eu-repo/semantics/altIdentifier/pmid/20732427 info:eu-repo/semantics/altIdentifier/wos/WOS:000283964000017 volume:172 issue:3 firstpage:343 lastpage:352 numberofpages:10 journal:JOURNAL OF STRUCTURAL BIOLOGY http://hdl.handle.net/11588/371041 doi:10.1016/j.jsb.2010.08.008 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-77958176737 http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WM5-50V20D3-2&_user=2607107&_coverDate=08%2F21%2F2010&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_acct=C000057976&_version=1&_urlVersion=0&_userid=2607107&md5=5261f061e0e3a5fbdec45a1a4d974192&searchtype=a info:eu-repo/semantics/closedAccess superoxide dismutase cold adaptation. X-ray crystallography info:eu-repo/semantics/article 2010 ftunivnapoliiris https://doi.org/10.1016/j.jsb.2010.08.008 2024-06-17T15:19:26Z Superoxide dismutases (SODs) are metalloenzymes catalysing the dismutation of superoxide anion radicals into molecular oxygen and hydrogen peroxide. Here, we present the crystal structure of a cold-adapted Fe-SOD from the Antarctic eubacterium Pseudoalteromonas haloplanktis (PhSOD), and that of its complex with sodium azide. The structures were compared with those of the corresponding homologues having a high sequence identity with PhSOD, such as the mesophilic SOD from Escherichia coli (EcSOD) or Pseudomonas ovalis, and the psychrophilic SOD from Aliivibrio salmonicida (AsSOD). These enzymes shared a large structural similarity, such as a conserved tertiary structure and arrangement of the two monomers, an almost identical total number of inter- and intramolecular hydrogen bonds and salt bridges. However, the two cold-adapted SODs showed an increased flexibility of the active site residues with respect to their mesophilic homologues. Structural information was combined with a characterisation of the chemical and thermal stability performed by CD and fluorescence measurements. Despite of its psychrophilic origin, the denaturation temperature of PhSOD was comparable with that of the mesophilic EcSOD, whereas AsSOD showed a lower denaturation temperature. On the contrary, the values of the denaturant concentration at the transition midpoint were in line with the psychrophilic/mesophilic origin of the proteins. These data provide additional support to the hypothesis that cold-adapted enzymes achieve efficient catalysis at low temperature, by increasing the flexibility of their active site; moreover, our results underline how fine structural modifications can alter enzyme flexibility and/or stability without compromising the overall structure of typical rigid enzymes, such as SODs. Article in Journal/Newspaper Antarc* Antarctic IRIS Università degli Studi di Napoli Federico II Antarctic The Antarctic Journal of Structural Biology 172 3 343 352 |
institution |
Open Polar |
collection |
IRIS Università degli Studi di Napoli Federico II |
op_collection_id |
ftunivnapoliiris |
language |
English |
topic |
superoxide dismutase cold adaptation. X-ray crystallography |
spellingShingle |
superoxide dismutase cold adaptation. X-ray crystallography MERLINO, ANTONELLO RUSSO KRAUSS, IRENE CASTELLANO, IMMACOLATA DE VENDITTIS, EMMANUELE VERGARA, ALESSANDRO SICA, FILOMENA B. Rossi M. Conte Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis |
topic_facet |
superoxide dismutase cold adaptation. X-ray crystallography |
description |
Superoxide dismutases (SODs) are metalloenzymes catalysing the dismutation of superoxide anion radicals into molecular oxygen and hydrogen peroxide. Here, we present the crystal structure of a cold-adapted Fe-SOD from the Antarctic eubacterium Pseudoalteromonas haloplanktis (PhSOD), and that of its complex with sodium azide. The structures were compared with those of the corresponding homologues having a high sequence identity with PhSOD, such as the mesophilic SOD from Escherichia coli (EcSOD) or Pseudomonas ovalis, and the psychrophilic SOD from Aliivibrio salmonicida (AsSOD). These enzymes shared a large structural similarity, such as a conserved tertiary structure and arrangement of the two monomers, an almost identical total number of inter- and intramolecular hydrogen bonds and salt bridges. However, the two cold-adapted SODs showed an increased flexibility of the active site residues with respect to their mesophilic homologues. Structural information was combined with a characterisation of the chemical and thermal stability performed by CD and fluorescence measurements. Despite of its psychrophilic origin, the denaturation temperature of PhSOD was comparable with that of the mesophilic EcSOD, whereas AsSOD showed a lower denaturation temperature. On the contrary, the values of the denaturant concentration at the transition midpoint were in line with the psychrophilic/mesophilic origin of the proteins. These data provide additional support to the hypothesis that cold-adapted enzymes achieve efficient catalysis at low temperature, by increasing the flexibility of their active site; moreover, our results underline how fine structural modifications can alter enzyme flexibility and/or stability without compromising the overall structure of typical rigid enzymes, such as SODs. |
author2 |
Merlino, Antonello RUSSO KRAUSS, Irene Castellano, Immacolata DE VENDITTIS, Emmanuele B., Rossi M., Conte Vergara, Alessandro Sica, Filomena |
format |
Article in Journal/Newspaper |
author |
MERLINO, ANTONELLO RUSSO KRAUSS, IRENE CASTELLANO, IMMACOLATA DE VENDITTIS, EMMANUELE VERGARA, ALESSANDRO SICA, FILOMENA B. Rossi M. Conte |
author_facet |
MERLINO, ANTONELLO RUSSO KRAUSS, IRENE CASTELLANO, IMMACOLATA DE VENDITTIS, EMMANUELE VERGARA, ALESSANDRO SICA, FILOMENA B. Rossi M. Conte |
author_sort |
MERLINO, ANTONELLO |
title |
Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis |
title_short |
Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis |
title_full |
Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis |
title_fullStr |
Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis |
title_full_unstemmed |
Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis |
title_sort |
structure and flexibility in cold-adapted iron superoxide dismutases: the case of the enzyme isolated from pseudoalteromonas haloplanktis |
publishDate |
2010 |
url |
http://hdl.handle.net/11588/371041 https://doi.org/10.1016/j.jsb.2010.08.008 http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WM5-50V20D3-2&_user=2607107&_coverDate=08%2F21%2F2010&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_acct=C000057976&_version=1&_urlVersion=0&_userid=2607107&md5=5261f061e0e3a5fbdec45a1a4d974192&searchtype=a |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/20732427 info:eu-repo/semantics/altIdentifier/wos/WOS:000283964000017 volume:172 issue:3 firstpage:343 lastpage:352 numberofpages:10 journal:JOURNAL OF STRUCTURAL BIOLOGY http://hdl.handle.net/11588/371041 doi:10.1016/j.jsb.2010.08.008 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-77958176737 http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WM5-50V20D3-2&_user=2607107&_coverDate=08%2F21%2F2010&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_acct=C000057976&_version=1&_urlVersion=0&_userid=2607107&md5=5261f061e0e3a5fbdec45a1a4d974192&searchtype=a |
op_rights |
info:eu-repo/semantics/closedAccess |
op_doi |
https://doi.org/10.1016/j.jsb.2010.08.008 |
container_title |
Journal of Structural Biology |
container_volume |
172 |
container_issue |
3 |
container_start_page |
343 |
op_container_end_page |
352 |
_version_ |
1809823199663226880 |