1b0i
From Proteopedia
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|PDB= 1b0i |SIZE=350|CAPTION= <scene name='initialview01'>1b0i</scene>, resolution 2.4Å | |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> | |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> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= AMY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=228 Pseudoalteromonas haloplanktis]) | |GENE= AMY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=228 Pseudoalteromonas haloplanktis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0i OCA], [http://www.ebi.ac.uk/pdbsum/1b0i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b0i RCSB]</span> | ||
}} | }} | ||
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[[Category: Aghajari, N.]] | [[Category: Aghajari, N.]] | ||
[[Category: Haser, R.]] | [[Category: Haser, R.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
[[Category: 4-glucan-4-glucanohydrolase]] | [[Category: 4-glucan-4-glucanohydrolase]] | ||
[[Category: alpha-1]] | [[Category: alpha-1]] | ||
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[[Category: psychrophilic enzyme]] | [[Category: psychrophilic enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:51:09 2008'' |
Revision as of 15:51, 30 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , | ||||||
| Gene: | AMY (Pseudoalteromonas haloplanktis) | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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