Characterization of a novel pectate lyase, Pel10A, from Pseudomonas cellulosa

Simon Charnock; Ian E. Brown; Johan Turkenburg; Gary Black; Gideon Davies

doi:10.1107/S0907444901007491

Characterization of a novel pectate lyase, Pel10A, from Pseudomonas cellulosa

Simon Charnock, Ian E. Brown, Johan Turkenburg, Gary Black, Gideon Davies

Applied Sciences Department

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

Biological recycling of plant material is essential for biosphere maintenance. This perpetual task involves a complex array of enzymes, including extracellular polysaccharide hydrolases and lyases. Whilst much is known about the structure and function of the hydrolases, relatively little is known about the structures and mechanisms of the corresponding lyases. To this end, crystals of the catalytic module of a novel family 10 pectate lyase, Pel10A from Pseudomonas cellulosa, were obtained using polyethylene glycol 2000 monomethylether as a precipitant. They belong to space group P21, with unit-cell parameters a = 47.7, b = 106.1, c = 55.4 Å, β = 92.0°, and have two molecules in the asymmetric unit. The crystals diffract beyond 1.5 Å using synchrotron radiation.

Original language	English
Pages (from-to)	1141-1143
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	57
Issue number	8
DOIs	https://doi.org/10.1107/S0907444901007491
Publication status	Published - 2001

Keywords

Pectate lyase

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10.1107/S0907444901007491

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title = "Characterization of a novel pectate lyase, Pel10A, from Pseudomonas cellulosa",

abstract = "Biological recycling of plant material is essential for biosphere maintenance. This perpetual task involves a complex array of enzymes, including extracellular polysaccharide hydrolases and lyases. Whilst much is known about the structure and function of the hydrolases, relatively little is known about the structures and mechanisms of the corresponding lyases. To this end, crystals of the catalytic module of a novel family 10 pectate lyase, Pel10A from Pseudomonas cellulosa, were obtained using polyethylene glycol 2000 monomethylether as a precipitant. They belong to space group P21, with unit-cell parameters a = 47.7, b = 106.1, c = 55.4 {\AA}, β = 92.0°, and have two molecules in the asymmetric unit. The crystals diffract beyond 1.5 {\AA} using synchrotron radiation.",

keywords = "Pectate lyase",

author = "Simon Charnock and Brown, {Ian E.} and Johan Turkenburg and Gary Black and Gideon Davies",

year = "2001",

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language = "English",

volume = "57",

pages = "1141--1143",

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TY - JOUR

T1 - Characterization of a novel pectate lyase, Pel10A, from Pseudomonas cellulosa

AU - Charnock, Simon

AU - Brown, Ian E.

AU - Turkenburg, Johan

AU - Black, Gary

AU - Davies, Gideon

PY - 2001

Y1 - 2001

N2 - Biological recycling of plant material is essential for biosphere maintenance. This perpetual task involves a complex array of enzymes, including extracellular polysaccharide hydrolases and lyases. Whilst much is known about the structure and function of the hydrolases, relatively little is known about the structures and mechanisms of the corresponding lyases. To this end, crystals of the catalytic module of a novel family 10 pectate lyase, Pel10A from Pseudomonas cellulosa, were obtained using polyethylene glycol 2000 monomethylether as a precipitant. They belong to space group P21, with unit-cell parameters a = 47.7, b = 106.1, c = 55.4 Å, β = 92.0°, and have two molecules in the asymmetric unit. The crystals diffract beyond 1.5 Å using synchrotron radiation.

AB - Biological recycling of plant material is essential for biosphere maintenance. This perpetual task involves a complex array of enzymes, including extracellular polysaccharide hydrolases and lyases. Whilst much is known about the structure and function of the hydrolases, relatively little is known about the structures and mechanisms of the corresponding lyases. To this end, crystals of the catalytic module of a novel family 10 pectate lyase, Pel10A from Pseudomonas cellulosa, were obtained using polyethylene glycol 2000 monomethylether as a precipitant. They belong to space group P21, with unit-cell parameters a = 47.7, b = 106.1, c = 55.4 Å, β = 92.0°, and have two molecules in the asymmetric unit. The crystals diffract beyond 1.5 Å using synchrotron radiation.

KW - Pectate lyase

U2 - 10.1107/S0907444901007491

DO - 10.1107/S0907444901007491

M3 - Article

SN - 0907-4449

VL - 57

SP - 1141

EP - 1143

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

IS - 8

ER -

Characterization of a novel pectate lyase, Pel10A, from Pseudomonas cellulosa

Abstract

Keywords

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