Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2CDP

Structure of a CBM6 in complex with neoagarohexaose

2CDP の概要
エントリーDOI10.2210/pdb2cdp/pdb
関連するPDBエントリー2CDO
分子名称BETA-AGARASE 1, 3,6-anhydro-alpha-L-galactopyranose-(1-3)-beta-D-galactopyranose-(1-4)-3,6-anhydro-alpha-L-galactopyranose-(1-3)-beta-D-galactopyranose-(1-4)-3,6-anhydro-alpha-L-galactopyranose-(1-3)-beta-D-galactopyranose, CALCIUM ION, ... (6 entities in total)
機能のキーワードcarbohydrate-binding module, hydrolase
由来する生物種SACCHAROPHAGUS DEGRADANS
タンパク質・核酸の鎖数4
化学式量合計72287.81
構造登録者
主引用文献Henshaw, J.,Horne, A.,Van Bueren, A.L.,Money, V.A.,Bolam, D.N.,Czjzek, M.,Ekborg, N.A.,Weiner, R.M.,Hutcheson, S.W.,Davies, G.J.,Boraston, A.B.,Gilbert, H.J.
Family 6 Carbohydrate Binding Modules in Beta-Agarases Display Exquisite Selectivity for the Non- Reducing Termini of Agarose Chains.
J.Biol.Chem., 281:17099-, 2006
Cited by
PubMed Abstract: Carbohydrate recognition is central to the biological and industrial exploitation of plant structural polysaccharides. These insoluble polymers are recalcitrant to microbial degradation, and enzymes that catalyze this process generally contain non-catalytic carbohydrate binding modules (CBMs) that potentiate activity by increasing substrate binding. Agarose, a repeat of the disaccharide 3,6-anhydro-alpha-L-galactose-(1,3)-beta-D-galactopyranose-(1,4), is the dominant matrix polysaccharide in marine algae, yet the role of CBMs in the hydrolysis of this important polymer has not previously been explored. Here we show that family 6 CBMs, present in two different beta-agarases, bind specifically to the non-reducing end of agarose chains, recognizing only the first repeat of the disaccharide. The crystal structure of one of these modules Aga16B-CBM6-2, in complex with neoagarohexaose, reveals the mechanism by which the protein displays exquisite specificity, targeting the equatorial O4 and the axial O3 of the anhydro-L-galactose. Targeting of the CBM6 to the non-reducing end of agarose chains may direct the appended catalytic modules to areas of the plant cell wall attacked by beta-agarases where the matrix polysaccharide is likely to be more amenable to further enzymic hydrolysis.
PubMed: 16601125
DOI: 10.1074/JBC.M600702200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.59 Å)
構造検証レポート
Validation report summary of 2cdp
検証レポート(詳細版)ダウンロードをダウンロード

249697

件を2026-02-25に公開中

PDB statisticsPDBj update infoContact PDBjnumon