1uuq
|
EXO-MANNOSIDASE FROM CELLVIBRIO MIXTUS
OverviewOverview
The enzymatic hydrolysis of the glycosidic bond is central to numerous, biological processes. Glycoside hydrolases, which catalyze these, reactions, are grouped into families based on primary sequence, similarities. One of the largest glycoside hydrolase families is glycoside, hydrolase family 5 (GH5), which contains primarily endo-acting enzymes, that hydrolyze beta-mannans and beta-glucans. Here we report the cloning, characterization, and three-dimensional structure of the Cellvibrio mixtus, GH5 beta-mannosidase (CmMan5A). This enzyme releases mannose from the, nonreducing end of mannooligosaccharides and polysaccharides, an activity, not previously observed in this enzyme family. CmMan5A contains a single, glycone (-1) and two aglycone (+1 and +2) sugar-binding subsites. The -1, ... [(full description)]
About this StructureAbout this Structure
1UUQ is a [Single protein] structure of sequence from [Cellvibrio mixtus] with SO4 and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Insights into the molecular determinants of substrate specificity in glycoside hydrolase family 5 revealed by the crystal structure and kinetics of Cellvibrio mixtus mannosidase 5A., Dias FM, Vincent F, Pell G, Prates JA, Centeno MS, Tailford LE, Ferreira LM, Fontes CM, Davies GJ, Gilbert HJ, J Biol Chem. 2004 Jun 11;279(24):25517-26. Epub 2004 Mar 10. PMID:15014076
Page seeded by OCA on Tue Oct 30 16:11:58 2007