1b0i: Difference between revisions
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[[Category: psychrophilic enzyme]] | [[Category: psychrophilic enzyme]] | ||
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Revision as of 15:48, 30 October 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 ... [(full description)]
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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