1b0i: Difference between revisions
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[[Image:1b0i.gif|left|200px]] | [[Image:1b0i.gif|left|200px]] | ||
'''ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS''' | {{Structure | ||
|PDB= 1b0i |SIZE=350|CAPTION= <scene name='initialview01'>1b0i</scene>, resolution 2.4Å | |||
|SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene>, <scene name='pdbsite=CAB:Ca+Binding+Site'>CAB</scene> and <scene name='pdbsite=CLB:Chloride+Binding+Site'>CLB</scene> | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= [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] | |||
|GENE= AMY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=228 Pseudoalteromonas haloplanktis]) | |||
}} | |||
'''ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1B0I is a [ | 1B0I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudoalteromonas_haloplanktis Pseudoalteromonas haloplanktis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0I OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9862804 9862804] | ||
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Pseudoalteromonas haloplanktis]] | [[Category: Pseudoalteromonas haloplanktis]] | ||
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[[Category: psychrophilic enzyme]] | [[Category: psychrophilic enzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:04:40 2008'' | ||
Revision as of 11:04, 20 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | and | ||||||
| Gene: | AMY (Pseudoalteromonas haloplanktis) | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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