This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1b0i
From Proteopedia
| Line 25: | Line 25: | ||
[[Category: psychrophilic enzyme]] | [[Category: psychrophilic enzyme]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:53:01 2007'' |
Revision as of 13:47, 5 November 2007
|
ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS
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 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
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.
Reference
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
Page seeded by OCA on Mon Nov 5 15:53:01 2007
