1b0i: Difference between revisions
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==Overview== | ==Overview== | ||
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 .. | 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. | ||
==About this Structure== | ==About this Structure== | ||
1B0I is a | 1B0I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudoalteromonas_haloplanktis Pseudoalteromonas haloplanktis] with CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Structure known Active Sites: ACT, CAB and CLB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B0I OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: psychrophilic enzyme]] | [[Category: psychrophilic enzyme]] | ||
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Revision as of 14:30, 5 November 2007
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ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS
OverviewOverview
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.
About this StructureAbout this Structure
1B0I is a Single protein structure of sequence from Pseudoalteromonas haloplanktis with CA and CL as ligands. Active as Alpha-amylase, with EC number 3.2.1.1 Structure known Active Sites: ACT, CAB and CLB. Full crystallographic information is available from OCA.
ReferenceReference
Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level., Aghajari N, Feller G, Gerday C, Haser R, Structure. 1998 Dec 15;6(12):1503-16. PMID:9862804
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