2c3x: Difference between revisions
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Revision as of 17:52, 30 October 2007
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STRUCTURE OF IODINATED CBM25 FROM BACILLUS HALODURANS AMYLASE IN COMPLEX WITH MALTOTETRAOSE
OverviewOverview
Starch-hydrolyzing enzymes lacking alpha-glucan-specific, carbohydrate-binding modules (CBMs) typically have lowered activity on, granular starch relative to their counterparts with CBMs. Thus, consideration of starch recognition by CBMs is a key factor in, understanding granular starch hydrolysis. To this end, we have dissected, the modular structure of the maltohexaose-forming amylase from Bacillus, halodurans (C-125). This five-module protein comprises an N-terminal, family 13 catalytic module followed in order by two modules of unknown, function, a family 26 CBM (BhCBM26), and a family 25 CBM (BhCBM25). Here, we present a comprehensive structure-function analysis of starch and, alpha-glucooligosaccharide recognition by BhCBM25 and BhCBM26 using UV, methods, isothermal titration ... [(full description)]
About this StructureAbout this Structure
2C3X is a [Single protein] structure of sequence from [Bacillus halodurans] with SO4 as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition., Boraston AB, Healey M, Klassen J, Ficko-Blean E, Lammerts van Bueren A, Law V, J Biol Chem. 2006 Jan 6;281(1):587-98. Epub 2005 Oct 17. PMID:16230347
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