1b0i

File:1b0i.gif

spinqualitylabelsall models 1b0i, resolution 2.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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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