Crystal structure of the Glu328Gln mutant of Neisseria polysaccharea amylosucrase in complex with sucrose and maltoheptaose

Lars K. Skov; Osman Mirza; Desiree Sprogøe; Bart van der Veen; Magali Remaud-Simeon; Cecile Albenne; Pierre Monsan; Michael Gajhede

doi:10.1080/10242420500538100

Crystal structure of the Glu328Gln mutant of Neisseria polysaccharea amylosucrase in complex with sucrose and maltoheptaose

Lars K. Skov^*, Osman Mirza, Desiree Sprogøe, Bart van der Veen, Magali Remaud-Simeon, Cecile Albenne, Pierre Monsan, Michael Gajhede

^*Corresponding author af dette arbejde

11 Citationer (Scopus)

Abstract

Several enzymes acting on sucrose are found in glycoside hydrolase family 13 (the α-amylase family). They all transfer a glucosyl moiety from sucrose to an acceptor, but the products can be very different. The structure of a variant of one of these, the Glu328Gln mutant of Neisseria polysaccharea amylosucrase, has been determined in a ternary complex with sucrose and an oligosaccharide to 2.16 Å resolution using x-ray crystallography. Sucrose selectively binds in the active site and the oligosaccharide only binds at surface sites. When this structure is compared to structures of other enzymes acting on sucrose from glycoside hydrolase family 13, it is found that the active site residues are very similar around the glucose part of sucrose while much variation is seen around the fructose moiety.

Originalsprog	Engelsk
Tidsskrift	Biocatalysis and Biotransformation
Vol/bind	24
Udgave nummer	1-2
Sider (fra-til)	99-105
Antal sider	7
ISSN	1024-2422
DOI	https://doi.org/10.1080/10242420500538100
Status	Udgivet - 1 jan. 2006

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title = "Crystal structure of the Glu328Gln mutant of Neisseria polysaccharea amylosucrase in complex with sucrose and maltoheptaose",

abstract = "Several enzymes acting on sucrose are found in glycoside hydrolase family 13 (the α-amylase family). They all transfer a glucosyl moiety from sucrose to an acceptor, but the products can be very different. The structure of a variant of one of these, the Glu328Gln mutant of Neisseria polysaccharea amylosucrase, has been determined in a ternary complex with sucrose and an oligosaccharide to 2.16 {\AA} resolution using x-ray crystallography. Sucrose selectively binds in the active site and the oligosaccharide only binds at surface sites. When this structure is compared to structures of other enzymes acting on sucrose from glycoside hydrolase family 13, it is found that the active site residues are very similar around the glucose part of sucrose while much variation is seen around the fructose moiety.",

keywords = "Amylosucrase, Polymerase, Structure/function analysis, Sucrose acting enzymes, Ternary complex",

author = "Skov, {Lars K.} and Osman Mirza and Desiree Sprog{\o}e and {van der Veen}, Bart and Magali Remaud-Simeon and Cecile Albenne and Pierre Monsan and Michael Gajhede",

year = "2006",

month = jan,

day = "1",

doi = "10.1080/10242420500538100",

language = "English",

volume = "24",

pages = "99--105",

journal = "Biocatalysis and Biotransformation",

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TY - JOUR

T1 - Crystal structure of the Glu328Gln mutant of Neisseria polysaccharea amylosucrase in complex with sucrose and maltoheptaose

AU - Skov, Lars K.

AU - Mirza, Osman

AU - Sprogøe, Desiree

AU - van der Veen, Bart

AU - Remaud-Simeon, Magali

AU - Albenne, Cecile

AU - Monsan, Pierre

AU - Gajhede, Michael

PY - 2006/1/1

Y1 - 2006/1/1

N2 - Several enzymes acting on sucrose are found in glycoside hydrolase family 13 (the α-amylase family). They all transfer a glucosyl moiety from sucrose to an acceptor, but the products can be very different. The structure of a variant of one of these, the Glu328Gln mutant of Neisseria polysaccharea amylosucrase, has been determined in a ternary complex with sucrose and an oligosaccharide to 2.16 Å resolution using x-ray crystallography. Sucrose selectively binds in the active site and the oligosaccharide only binds at surface sites. When this structure is compared to structures of other enzymes acting on sucrose from glycoside hydrolase family 13, it is found that the active site residues are very similar around the glucose part of sucrose while much variation is seen around the fructose moiety.

AB - Several enzymes acting on sucrose are found in glycoside hydrolase family 13 (the α-amylase family). They all transfer a glucosyl moiety from sucrose to an acceptor, but the products can be very different. The structure of a variant of one of these, the Glu328Gln mutant of Neisseria polysaccharea amylosucrase, has been determined in a ternary complex with sucrose and an oligosaccharide to 2.16 Å resolution using x-ray crystallography. Sucrose selectively binds in the active site and the oligosaccharide only binds at surface sites. When this structure is compared to structures of other enzymes acting on sucrose from glycoside hydrolase family 13, it is found that the active site residues are very similar around the glucose part of sucrose while much variation is seen around the fructose moiety.

KW - Amylosucrase

KW - Polymerase

KW - Structure/function analysis

KW - Sucrose acting enzymes

KW - Ternary complex

UR - http://www.scopus.com/inward/record.url?scp=33646840522&partnerID=8YFLogxK

U2 - 10.1080/10242420500538100

DO - 10.1080/10242420500538100

M3 - Journal article

AN - SCOPUS:33646840522

SN - 1024-2422

VL - 24

SP - 99

EP - 105

JO - Biocatalysis and Biotransformation

JF - Biocatalysis and Biotransformation

IS - 1-2

ER -

Crystal structure of the Glu328Gln mutant of Neisseria polysaccharea amylosucrase in complex with sucrose and maltoheptaose

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