Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition.

Abstract:

:Here we report the first crystal structure of a protein, AmyA, a secretory alpha-amylase isolated from Halothermothrix orenii, which is both halophilic and thermophilic. The crystal structure was determined at 1.6 A resolution. AmyA lacks the conserved acidic surface, which is considered essential for protein stability at high salinity. Sedimentation velocity and CD experiments on AmyA reveal the formation of unique reversible poly-dispersed oligomers that show unusually high thermal stability. These studies provide valuable insight into the structural elements that contribute to the stability of AmyA at both physical and chemical extremes and their functional implications.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Sivakumar N,Li N,Tang JW,Patel BK,Swaminathan K

doi

10.1016/j.febslet.2006.04.017

subject

Has Abstract

pub_date

2006-05-15 00:00:00

pages

2646-52

issue

11

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)00438-8

journal_volume

580

pub_type

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