1b0i
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1b0i.gif|left|200px]] | [[Image:1b0i.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1b0i", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1b0i| PDB=1b0i | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS''' | '''ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS''' | ||
| Line 29: | Line 26: | ||
[[Category: Haser, R.]] | [[Category: Haser, R.]] | ||
[[Category: 4-glucan-4-glucanohydrolase]] | [[Category: 4-glucan-4-glucanohydrolase]] | ||
| - | [[Category: | + | [[Category: Alpha-1]] |
| - | [[Category: | + | [[Category: Alpha-amylase]] |
| - | [[Category: | + | [[Category: Beta-alpha-eight barrel]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 07:55, 2 May 2008
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. 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 Fri May 2 10:55:18 2008
