This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2bgp
From Proteopedia
|
MANNAN BINDING MODULE FROM MAN5C IN BOUND CONFORMATION
Overview
Enzymes that digest plant cell wall polysaccharides generally contain, non-catalytic, carbohydrate-binding modules (CBMs) that function by, attaching the enzyme to the substrate, potentiating catalytic activity., Here, we present the first structure of a family 35 CBM, derived from the, Cellvibrio japonicus beta-1,4-mannanase Man5C. The NMR structure has been, determined for both the free protein and the protein bound to, mannopentaose. The data show that the protein displays a typical, beta-jelly-roll fold. Ligand binding is not located on the concave surface, of the protein, as occurs in many CBMs that display the jelly-roll fold, but is formed by the loops that link the two beta-sheets of the protein, similar to family 6 CBMs. In contrast to the majority of CBMs, which are, generally ... [(full description)]
About this Structure
2BGP is a [Single protein] structure of sequence from [Cellvibrio japonicus]. Structure known Active Site: M. Full crystallographic information is available from [OCA].
Reference
Structure of a mannan-specific family 35 carbohydrate-binding module: evidence for significant conformational changes upon ligand binding., Tunnicliffe RB, Bolam DN, Pell G, Gilbert HJ, Williamson MP, J Mol Biol. 2005 Mar 25;347(2):287-96. PMID:15740741
Page seeded by OCA on Tue Oct 30 08:45:50 2007
