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Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose.

Chaen K, Noguchi J, Omori T, Kakuta Y, Kimura M
Biochem Biophys Res Commun 424 508-11 (2012)
Cited: 16 times
EuropePMC logo PMID: 22771800

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.

Reviews - 3vu2 mentioned but not cited (1)

  1. Functional Roles of Starch Binding Domains and Surface Binding Sites in Enzymes Involved in Starch Biosynthesis. Wilkens C, Svensson B, Møller MS. Front Plant Sci 9 1652 (2018)

Articles - 3vu2 mentioned but not cited (3)

  1. Bound Substrate in the Structure of Cyanobacterial Branching Enzyme Supports a New Mechanistic Model. Hayashi M, Suzuki R, Colleoni C, Ball SG, Fujita N, Suzuki E. J Biol Chem 292 5465-5475 (2017)
  2. The characterization of modified starch branching enzymes: toward the control of starch chain-length distributions. Li C, Wu AC, Go RM, Malouf J, Turner MS, Malde AK, Mark AE, Gilbert RG. PLoS One 10 e0125507 (2015)
  3. A structural explanation for the mechanism and specificity of plant branching enzymes I and IIb. Gavgani HN, Fawaz R, Ehyaei N, Walls D, Pawlowski K, Fulgos R, Park S, Assar Z, Ghanbarpour A, Geiger JH. J Biol Chem 298 101395 (2022)


Reviews citing this publication (3)

  1. Structure and function of α-glucan debranching enzymes. Møller MS, Henriksen A, Svensson B. Cell Mol Life Sci 73 2619-2641 (2016)
  2. Progress in controlling starch structure by modifying starch-branching enzymes. Li C, Gilbert RG. Planta 243 13-22 (2016)
  3. Distribution of glucan-branching enzymes among prokaryotes. Suzuki E, Suzuki R. Cell Mol Life Sci 73 2643-2660 (2016)

Articles citing this publication (9)

  1. FLOURY ENDOSPERM6 encodes a CBM48 domain-containing protein involved in compound granule formation and starch synthesis in rice endosperm. Peng C, Wang Y, Liu F, Ren Y, Zhou K, Lv J, Zheng M, Zhao S, Zhang L, Wang C, Jiang L, Zhang X, Guo X, Bao Y, Wan J. Plant J 77 917-930 (2014)
  2. SnRK1 from Arabidopsis thaliana is an atypical AMPK. Emanuelle S, Hossain MI, Moller IE, Pedersen HL, van de Meene AM, Doblin MS, Koay A, Oakhill JS, Scott JW, Willats WG, Kemp BE, Bacic A, Gooley PR, Stapleton DI. Plant J 82 183-192 (2015)
  3. Evolutionary, structural and expression analysis of core genes involved in starch synthesis. Qu J, Xu S, Zhang Z, Chen G, Zhong Y, Liu L, Zhang R, Xue J, Guo D. Sci Rep 8 12736 (2018)
  4. Structural basis of glycogen branching enzyme deficiency and pharmacologic rescue by rational peptide design. Froese DS, Michaeli A, McCorvie TJ, Krojer T, Sasi M, Melaev E, Goldblum A, Zatsepin M, Lossos A, Álvarez R, Escribá PV, Minassian BA, von Delft F, Kakhlon O, Yue WW. Hum Mol Genet 24 5667-5676 (2015)
  5. Structure and Mechanism of Staphylococcus aureus TarS, the Wall Teichoic Acid β-glycosyltransferase Involved in Methicillin Resistance. Sobhanifar S, Worrall LJ, King DT, Wasney GA, Baumann L, Gale RT, Nosella M, Brown ED, Withers SG, Strynadka NC. PLoS Pathog 12 e1006067 (2016)
  6. Theoretical and experimental approaches to understand the biosynthesis of starch granules in a physiological context. Pfister B, Zeeman SC, Rugen MD, Field RA, Ebenhöh O, Raguin A. Photosynth Res 145 55-70 (2020)
  7. Phylogeny-structured carbohydrate metabolism across microbiomes collected from different units in wastewater treatment process. Xia Y, Chin FY, Chao Y, Zhang T. Biotechnol Biofuels 8 172 (2015)
  8. Alanine 310 is important for the activity of 1,4-α-glucan branching enzyme from Geobacillus thermoglucosidans STB02. Liu Y, Li C, Gu Z, Xin C, Cheng L, Hong Y, Li Z. Int J Biol Macromol 97 156-163 (2017)
  9. Origin and evolution of the main starch biosynthetic enzymes. Chang H, Bai J, Zhang H, Huang R, Chu H, Wang Q, Liu H, Cheng J, Jiang H. Synth Syst Biotechnol 8 462-468 (2023)


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