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PDBsum entry 1b0i

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Hydrolase PDB id
1b0i
Jmol
Contents
Protein chain
448 a.a. *
Metals
_CL
_CA
Waters ×303
* Residue conservation analysis

References listed in PDB file
Key reference
Title Structures of the psychrophilic alteromonas haloplanctis alpha-Amylase give insights into cold adaptation at a molecular level.
Authors N.Aghajari, G.Feller, C.Gerday, R.Haser.
Ref. Structure, 1998, 6, 1503-1516. [DOI no: 10.1016/S0969-2126(98)00149-X]
PubMed id 9862804
Abstract
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.
Figure 4.
Figure 4. A representation of charges at the surfaces of (a) AHA, (b) HPA and (c) BLA, displayed at the same potential range. Color codes are: red, aspartic and glutamic acids; blue, lysines and arginines. This figure was generated with the program GRASP [57].
The above figure is reprinted by permission from Cell Press: Structure (1998, 6, 1503-1516) copyright 1998.
Secondary reference #1
Title Crystal structures of the psychrophilic alpha-Amylase from alteromonas haloplanctis in its native form and complexed with an inhibitor.
Authors N.Aghajari, G.Feller, C.Gerday, R.Haser.
Ref. Protein Sci, 1998, 7, 564-572. [DOI no: 10.1002/pro.5560070304]
PubMed id 9541387
Full text Abstract
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