Sandbox Reserved 301

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

IntroductionIntroduction

spinqualitylabelsall models PDB ID 1m7x Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1m7x, resolution 2.30Å ()
Activity:	1,4-alpha-glucan branching enzyme, with EC number 2.4.1.18
Structural annotation: Resources: CATH : 1M7Xa02, 1M7Xa01, 1M7Xa03, 1M7Xb03, 1M7Xb02, 1M7Xb01, 1M7Xc02, 1M7Xc03, 1M7Xc01, 1M7Xd02, 1M7Xd01, 1M7Xd03 InterPro : Ipr006047, Ipr004193, Ipr006407, Ipr013780, Ipr013783, Ipr013781, Ipr014756, Ipr006048, Ipr013782 Pfam : PF02922, PF00128, PF02806 SCOP : d1m7xa2, d1m7xa1, d1m7xa3, d1m7xb3, d1m7xb1, d1m7xb2, d1m7xc1, d1m7xc3, d1m7xc2, d1m7xd1, d1m7xd2, d1m7xd3 UniProt : P07762
Functional annotation: Biological process: carbohydrate metabolic process glycogen biosynthetic process Molecular function: catalytic activity hydrolase activity, hydrolyzing O-glycosyl compounds 1,4-alpha-glucan branching enzyme activity cation binding transferase activity transferase activity, transferring glycosyl groups
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site. The branching enzyme belongs to the a-amylase family of enzymes.

FunctionFunction

Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell.

Glyogen Storage Disease type IVGlyogen Storage Disease type IV

Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system.

FamilyFamily

E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres, a-amylase, isoamylase, and

spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ReferencesReferences

E.ColiBranchingEnzyme