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1aqm

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Revision as of 16:36, 29 October 2007 by OCA (Talk | contribs)
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1aqm, resolution 1.85Å

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ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS COMPLEXED WITH TRIS

Overview

Alteromonas haloplanctis is a bacterium that flourishes in Antarctic, sea-water and it is considered as an extreme psychrophile. We have, determined the crystal structures of the alpha-amylase (AHA) secreted by, this bacterium, in its native state to 2.0 angstroms resolution as well as, in complex with Tris to 1.85 angstroms resolution. The structure of AHA, which is the first experimentally determined three-dimensional structure, of a psychrophilic enzyme, resembles those of other known alpha-amylases, of various origins with a surprisingly greatest similarity to mammalian, alpha-amylases. AHA contains a chloride ion which activates the hydrolytic, cleavage of substrate alpha-1,4-glycosidic bonds. The chloride binding, site is situated approximately 5 angstroms from the active site which ... [(full description)]

About this Structure

1AQM is a [Single protein] structure of sequence from [Pseudoalteromonas haloplanktis] with CA, CL and TRS as [ligands]. Active as [[1]], with EC number [3.2.1.1]. Full crystallographic information is available from [OCA].

Reference

Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor., Aghajari N, Feller G, Gerday C, Haser R, Protein Sci. 1998 Mar;7(3):564-72. PMID:9541387

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