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

S J  Charnock; I E  Brown; J P  Turkenburg; G W  Black; G J  Davies

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

S J Charnock, I E Brown, J P Turkenburg, G W Black, G J Davies

Chemistry

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

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 P2(1), with unit-cell parameters a = 47.7, b = 106.1, c = 55.4 Angstrom, beta = 92.0 degrees, and have two molecules in the asymmetric unit. The crystals diffract beyond 1.5 Angstrom using synchrotron radiation.

Original language	English
Pages (from-to)	1141-1143
Number of pages	3
Journal	Acta Crystallographica. Section D, Biological Crystallography
Volume	57
Publication status	Published - Aug 2001

Keywords

NUCLEOTIDE
ENZYMES
ERWINIA

Cite this

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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 P2(1), with unit-cell parameters a = 47.7, b = 106.1, c = 55.4 Angstrom, beta = 92.0 degrees, and have two molecules in the asymmetric unit. The crystals diffract beyond 1.5 Angstrom using synchrotron radiation.",

keywords = "NUCLEOTIDE, ENZYMES, ERWINIA",

author = "Charnock, {S J} and Brown, {I E} and Turkenburg, {J P} and Black, {G W} and Davies, {G J}",

year = "2001",

month = aug,

language = "English",

volume = "57",

pages = "1141--1143",

journal = "Acta Crystallographica. Section D, Biological Crystallography",

issn = "0907-4449",

publisher = "International Union of Crystallography",

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TY - JOUR

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

AU - Charnock, S J

AU - Brown, I E

AU - Turkenburg, J P

AU - Black, G W

AU - Davies, G J

PY - 2001/8

Y1 - 2001/8

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 P2(1), with unit-cell parameters a = 47.7, b = 106.1, c = 55.4 Angstrom, beta = 92.0 degrees, and have two molecules in the asymmetric unit. The crystals diffract beyond 1.5 Angstrom 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 P2(1), with unit-cell parameters a = 47.7, b = 106.1, c = 55.4 Angstrom, beta = 92.0 degrees, and have two molecules in the asymmetric unit. The crystals diffract beyond 1.5 Angstrom using synchrotron radiation.

KW - NUCLEOTIDE

KW - ENZYMES

KW - ERWINIA

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

ER -