Crystal Structures of Escherichia coli Branching Enzyme in Complex with Linear Oligosaccharides

Feng, Lei; Fawaz, Remie; Hovde, Stacy; Gilbert, Lindsey; Chiou, Janice; Geiger, James H.

doi:10.1021/acs.biochem.5b00228

Title: Crystal Structures of Escherichia coli Branching Enzyme in Complex with Linear Oligosaccharides

Journal Article · Mon Aug 17 00:00:00 EDT 2015 · Biochemistry

DOI:https://doi.org/10.1021/acs.biochem.5b00228· OSTI ID:1223543

Feng, Lei ^[1]; Fawaz, Remie ^[1]; Hovde, Stacy ^[2]; Gilbert, Lindsey ^[1]; Chiou, Janice ^[1]; Geiger, James H. ^[1]

Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States
Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States, Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States

Branching enzyme is responsible for all branching of glycogen and starch. It is an unusual member of the α-amylase family because it has both α-1,4-amylase activity and α-1,6-transferase activity. It also does not react with shorter glucans, though it will bind much longer substrates and substrate mimics. In an effort to better understand how branching enzyme interacts with its polymeric substrate, we have determined the structure of Δ112 Escherichia coli branching enzyme bound to maltoheptaose and maltohexaose. Together, these structures define six distinct oligosaccharide binding sites on the surface of E. coli branching enzyme. Most of these binding sites surround the edge of the β-barrel domain and are quite far from the active site. Surprisingly, there is no evidence of oligosaccharide binding in the active site of the enzyme. The closest bound oligosaccharide resides almost 18 Å from the active site. Mutations to conserved residues in binding sites I and VI had a debilitating effect on the activity of the enzyme.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences, and Biosciences Division

Grant/Contract Number:: FG02-06ER15822

OSTI ID:: 1223543

Alternate ID(s):: OSTI ID: 1498300

Journal Information:: Biochemistry, Journal Name: Biochemistry Vol. 54 Journal Issue: 40; ISSN 0006-2960

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 41 works

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