Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.febslet.2006.04.017
DC FieldValue
dc.titleCrystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition
dc.contributor.authorSivakumar, N.
dc.contributor.authorLi, N.
dc.contributor.authorTang, J.W.
dc.contributor.authorPatel, B.K.C.
dc.contributor.authorSwaminathan, K.
dc.date.accessioned2014-10-27T08:24:55Z
dc.date.available2014-10-27T08:24:55Z
dc.date.issued2006-05-15
dc.identifier.citationSivakumar, N., Li, N., Tang, J.W., Patel, B.K.C., Swaminathan, K. (2006-05-15). Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition. FEBS Letters 580 (11) : 2646-2652. ScholarBank@NUS Repository. https://doi.org/10.1016/j.febslet.2006.04.017
dc.identifier.issn00145793
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100357
dc.description.abstractHere we report the first crystal structure of a protein, AmyA, a secretory α-amylase isolated from Halothermothrix orenii, which is both halophilic and thermophilic. The crystal structure was determined at 1.6 Å 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. © 2006.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.febslet.2006.04.017
dc.sourceScopus
dc.subjectAmylase
dc.subjectHalophilic
dc.subjectOligomerization
dc.subjectPoly-extreme
dc.subjectThermophilic
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/j.febslet.2006.04.017
dc.description.sourcetitleFEBS Letters
dc.description.volume580
dc.description.issue11
dc.description.page2646-2652
dc.description.codenFEBLA
dc.identifier.isiut000237686400018
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

43
checked on Jul 12, 2019

WEB OF SCIENCETM
Citations

44
checked on Jul 12, 2019

Page view(s)

73
checked on Jun 21, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.