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| {{STRUCTURE_1b0i| PDB=1b0i | SCENE= }} | | {{STRUCTURE_1b0i| PDB=1b0i | SCENE= }} |
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| '''ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS'''
| | ===ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS=== |
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| ==Overview==
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| Background:. Enzymes from psychrophilic (cold-adapted) microorganisms operate at temperatures close to 0 degreesC, where the activity of their mesophilic and thermophilic counterparts is drastically reduced. It has generally been assumed that thermophily is associated with rigid proteins, whereas psychrophilic enzymes have a tendency to be more flexible. Results:. Insights into the cold adaptation of proteins are gained on the basis of a psychrophilic protein's molecular structure. To this end, we have determined the structure of the recombinant form of a psychrophilic alpha-amylase from Alteromonas haloplanctis at 2.4 A resolution. We have compared this with the structure of the wild-type enzyme, recently solved at 2.0 A resolution, and with available structures of their mesophilic counterparts. These comparative studies have enabled us to identify possible determinants of cold adaptation. Conclusions:. We propose that an increased resilience of the molecular surface and a less rigid protein core, with less interdomain interactions, are determining factors of the conformational flexibility that allows efficient enzyme catalysis in cold environments.
| | The line below this paragraph, {{ABSTRACT_PUBMED_9862804}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9862804 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9862804}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Beta-alpha-eight barrel]] | | [[Category: Beta-alpha-eight barrel]] |
| [[Category: Psychrophilic enzyme]] | | [[Category: Psychrophilic enzyme]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:55:18 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:59:07 2008'' |
