3VU2

Structure of the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L

Summary for 3VU2

• Entry DOI: 10.2210/pdb3vu2/pdb
• Related: 3AMK
• Related PRD ID: PRD_900030
• Descriptor: 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: carbohydrate-binding module 48, transferase
• Biological source: Oryza sativa Japonica Group (Japanese rice)
• Cellular location: Plastid, chloroplast: Q01401
• Total number of polymer chains: 2
• Total formula weight: 165241.69

Authors

Chaen, K.,Kakuta, Y.,Kimura, M. (deposition date: 2012-06-14, release date: 2013-05-08, Last modification date: 2024-03-20)

Primary citation

Chaen, K.,Noguchi, J.,Omori, T.,Kakuta, Y.,Kimura, M.
Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose.
Biochem.Biophys.Res.Commun., 424:508-511, 2012

PubMed Abstract: Starch branching enzyme (SBE) catalyzes the cleavage of α-1,4-linkages and the subsequent transfer of α-1,4 glucan to form an α-1,6 branch point in amylopectin. We determined the crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose at a resolution of 2.2Å. Maltopentaose bound to a hydrophobic pocket formed by the N-terminal helix, carbohydrate-binding module 48 (CBM48), and α-amylase domain. In addition, glucose moieties could be observed at molecular surfaces on the N-terminal helix (α2) and CBM48. Amino acid residues involved in the carbohydrate bindings are highly conserved in other SBEs, suggesting their generally conserved role in substrate binding for SBEs.

PubMed: 22771800
DOI: 10.1016/j.bbrc.2012.06.145

Experimental method

X-RAY DIFFRACTION (2.23 Å)