1bli

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[[Category: thermostability]]
[[Category: thermostability]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:51:23 2007''
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Revision as of 12:51, 30 October 2007


1bli, resolution 1.90Å

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BACILLUS LICHENIFORMIS ALPHA-AMYLASE

Overview

BACKGROUND: The structural basis as to how metals regulate the functional, state of a protein by altering or stabilizing its conformation has been, characterized in relatively few cases because the metal-free form of the, protein is often partially disordered and unsuitable for crystallographic, analysis. This is not the case, however, for Bacillus licheniformis, alpha-amylase (BLA) for which the structure of the metal-free form is, available. BLA is a hyperthermostable enzyme which is widely used in, biotechnology, for example in the breakdown of starch or as a component of, detergents. The determination of the structure of BLA in the, metal-containing form, together with comparisons to the apo enzyme, will, help us to understand the way in which metal ions can regulate enzyme, activity. ... [(full description)]

About this Structure

1BLI is a [Single protein] structure of sequence from [Bacillus licheniformis] with CA and NA as [ligands]. Active as [Alpha-amylase], with EC number [3.2.1.1]. Structure known Active Sites: CA1, CA2, CA3, CS and NA1. Full crystallographic information is available from [OCA].

Reference

Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad., Machius M, Declerck N, Huber R, Wiegand G, Structure. 1998 Mar 15;6(3):281-92. PMID:9551551

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