2c3v
From Proteopedia
| Line 29: | Line 29: | ||
[[Category: starch binding]] | [[Category: starch binding]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:57:01 2007'' |
Revision as of 14:52, 30 October 2007
|
STRUCTURE OF IODINATED CBM25 FROM BACILLUS HALODURANS AMYLASE
Overview
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 Structure
2C3V is a [Protein complex] structure of sequences from [Bacillus halodurans] with IOD as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Tue Oct 30 16:57:01 2007
