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1B0I

ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS

Summary for 1B0I
Entry DOI10.2210/pdb1b0i/pdb
DescriptorPROTEIN (ALPHA-AMYLASE), CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsalpha-amylase, alpha-1, 4-glucan-4-glucanohydrolase, beta-alpha-eight barrel, psychrophilic enzyme, hydrolase
Biological sourcePseudoalteromonas haloplanktis
Cellular locationSecreted : P29957
Total number of polymer chains1
Total formula weight49456.37
Authors
Aghajari, N.,Haser, R. (deposition date: 1998-11-10, release date: 1999-11-17, Last modification date: 2024-11-13)
Primary citationAghajari, N.,Feller, G.,Gerday, C.,Haser, R.
Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level.
Structure, 6:1503-1506, 1998
Cited by
PubMed Abstract: . 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.
PubMed: 9862804
DOI: 10.1016/S0969-2126(98)00149-X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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